Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.
Proteins encoded by the CHLOROPLAST GENOME or proteins encoded by the nuclear genome that are imported to and resident in the CHOROPLASTS.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
A variable annual leguminous vine (Pisum sativum) that is cultivated for its rounded smooth or wrinkled edible protein-rich seeds, the seed of the pea, and the immature pods with their included seeds. (From Webster's New Collegiate Dictionary, 1973)
Deoxyribonucleic acid that makes up the genetic material of CHLOROPLASTS.
Ribonucleic acid in chloroplasts having regulatory and catalytic roles as well as involvement in protein synthesis.
A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. It can also utilize OXYGEN as a substrate to catalyze the synthesis of 2-phosphoglycolate and 3-phosphoglycerate in a process referred to as photorespiration.
Membranous cisternae of the CHLOROPLAST containing photosynthetic pigments, reaction centers, and the electron-transport chain. Each thylakoid consists of a flattened sac of membrane enclosing a narrow intra-thylakoid space (Lackie and Dow, Dictionary of Cell Biology, 2nd ed). Individual thylakoids are interconnected and tend to stack to form aggregates called grana. They are found in cyanobacteria and all plants.
The genetic complement of CHLOROPLASTS as represented in their DNA.
Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms.
The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.
Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.
A genus GREEN ALGAE in the order VOLVOCIDA. It consists of solitary biflagellated organisms common in fresh water and damp soil.
A species of GREEN ALGAE. Delicate, hairlike appendages arise from the flagellar surface in these organisms.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
A species of fresh-water, flagellated EUKARYOTES in the phylum EUGLENIDA.
Self-replicating cytoplasmic organelles of plant and algal cells that contain pigments and may synthesize and accumulate various substances. PLASTID GENOMES are used in phylogenetic studies.
A subtype of thioredoxins found primarily in CHLOROPLASTS.
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
A genus of EUKARYOTES, in the phylum EUGLENIDA, found mostly in stagnant water. Characteristics include a pellicle usually marked by spiral or longitudinal striations.
A large multisubunit protein complex found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to catalyze the splitting of WATER into DIOXYGEN and of reducing equivalents of HYDROGEN.
Proteins found in any species of algae.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)
Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.
Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
Complexes containing CHLOROPHYLL and other photosensitive molecules. They serve to capture energy in the form of PHOTONS and are generally found as components of the PHOTOSYSTEM I PROTEIN COMPLEX or the PHOTOSYSTEM II PROTEIN COMPLEX.
Protein precursors, also known as proproteins or prohormones, are inactive forms of proteins that undergo post-translational modification, such as cleavage, to produce the active functional protein or peptide hormone.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The large family of plants characterized by pods. Some are edible and some cause LATHYRISM or FAVISM and other forms of poisoning. Other species yield useful materials like gums from ACACIA and various LECTINS like PHYTOHEMAGGLUTININS from PHASEOLUS. Many of them harbor NITROGEN FIXATION bacteria on their roots. Many but not all species of "beans" belong to this family.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
PLANTS, or their progeny, whose GENOME has been altered by GENETIC ENGINEERING.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Those nucleic acid sequences that function as units of heredity which are located within the CHLOROPLAST DNA.
Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
The functional hereditary units of PLANTS.
A plant genus of the family SOLANACEAE. Members contain NICOTINE and other biologically active chemicals; its dried leaves are used for SMOKING.
Ribonucleic acid in plants having regulatory and catalytic roles as well as involvement in protein synthesis.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
The absence of light.
Proton-translocating ATPases which produce ADENOSINE TRIPHOSPHATE in plants. They derive energy from light-driven reactions that develop high concentrations of protons within the membranous cisternae (THYLAKOIDS) of the CHLOROPLASTS.
A plant species of the family POACEAE. It is a tall grass grown for its EDIBLE GRAIN, corn, used as food and animal FODDER.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A large multisubunit protein complex that is found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to drive electron transfer reactions that result in either the reduction of NADP to NADPH or the transport of PROTONS across the membrane.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The relationships of groups of organisms as reflected by their genetic makeup.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A phylum of photosynthetic EUKARYOTA bearing double membrane-bound plastids containing chlorophyll a and b. They comprise the classical green algae, and represent over 7000 species that live in a variety of primarily aquatic habitats. Only about ten percent are marine species, most live in freshwater.
Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.
The use of light to convert ADP to ATP without the concomitant reduction of dioxygen to water as occurs during OXIDATIVE PHOSPHORYLATION in MITOCHONDRIA.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
A group of GLYCOLIPIDS in which the sugar group is GALACTOSE. They are distinguished from GLYCOSPHINGOLIPIDS in lacking nitrogen. They constitute the majority of MEMBRANE LIPIDS in PLANTS.
A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the first electrophoresis. This technique is usually performed on polyacrylamide gels.
A protein complex that includes CYTOCHROME B6 and CYTOCHROME F. It is found in the THYLAKOID MEMBRANE and plays an important role in process of PHOTOSYNTHESIS by transferring electrons from PLASTOQUINONE to PLASTOCYANIN or CYTOCHROME C6. The transfer of electrons is coupled to the transport of PROTONS across the membrane.
Deoxyribonucleic acid that makes up the genetic material of plants.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The sum of the weight of all the atoms in a molecule.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
One of the three domains of life (the others being BACTERIA and ARCHAEA), also called Eukarya. These are organisms whose cells are enclosed in membranes and possess a nucleus. They comprise almost all multicellular and many unicellular organisms, and are traditionally divided into groups (sometimes called kingdoms) including ANIMALS; PLANTS; FUNGI; and various algae and other taxa that were previously part of the old kingdom Protista.
Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.
Cytochromes f are found as components of the CYTOCHROME B6F COMPLEX. They play important role in the transfer of electrons from PHOTOSYSTEM I to PHOTOSYSTEM II.
Plants or plant parts which are harmful to man or other animals.
The genetic complement of a plant (PLANTS) as represented in its DNA.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Large and highly vacuolated cells possessing many chloroplasts occuring in the interior cross-section of leaves, juxtaposed between the epidermal layers.
A pre-emergent herbicide.
An organism of the vegetable kingdom suitable by nature for use as a food, especially by human beings. Not all parts of any given plant are edible but all parts of edible plants have been known to figure as raw or cooked food: leaves, roots, tubers, stems, seeds, buds, fruits, and flowers. The most commonly edible parts of plants are FRUIT, usually sweet, fleshy, and succulent. Most edible plants are commonly cultivated for their nutritional value and are referred to as VEGETABLES.
A genus of green algae found in the Mediterranean and other warm seas.
A plant genus of the family POACEAE. The EDIBLE GRAIN, barley, is widely used as food.
A process that changes the nucleotide sequence of mRNA from that of the DNA template encoding it. Some major classes of RNA editing are as follows: 1, the conversion of cytosine to uracil in mRNA; 2, the addition of variable number of guanines at pre-determined sites; and 3, the addition and deletion of uracils, templated by guide-RNAs (RNA, GUIDE).
Polyunsaturated side-chain quinone derivative which is an important link in the electron transport chain of green plants during the photosynthetic conversion of light energy by photophosphorylation into the potential energy of chemical bonds.
Members of the group of vascular plants which bear flowers. They are differentiated from GYMNOSPERMS by their production of seeds within a closed chamber (OVARY, PLANT). The Angiosperms division is composed of two classes, the monocotyledons (Liliopsida) and dicotyledons (Magnoliopsida). Angiosperms represent approximately 80% of all known living plants.
Ribonucleic acid in algae having regulatory and catalytic roles as well as involvement in protein synthesis.
An enzyme that catalyzes the conversion of D-fructose 1,6-bisphosphate and water to D-fructose 6-phosphate and orthophosphate. EC
A copper-containing plant protein that is a fundamental link in the electron transport chain of green plants during the photosynthetic conversion of light energy by photophosphorylation into the potential energy of chemical bonds.
A subcategory of chaperonins found in MITOCHONDRIA; CHLOROPLASTS; and BACTERIA. Group I chaperonins form into a barrel-shaped macromolecular structure that is enclosed by a separate lid-like protein component.

Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids. (1/207)

All plant cells contain plastids. Various reactions are located exclusively within these unique organelles, requiring the controlled exchange of a wide range of solutes, ions, and metabolites. In recent years, several proteins involved in import and/or export of these compounds have been characterized using biochemical and electrophysiological approaches, and in addition have been identified at the molecular level. Several solute channels have been identified in the outer envelope membrane. These porin-like proteins in the outer envelope membrane were formerly thought to be quite unspecific, but have now been shown to exhibit significant substrate specificity and to be highly regulated. Therefore, the inter-envelope membrane space is not as freely accessible as previously thought. Transport proteins in the inner envelope membrane have been characterized in more detail. It has been proved unequivocally that a family of proteins (including triose phosphate-/phosphoenolpyruvate-, and glucose 6-phosphate-specific transporters) permit the exchange of inorganic phosphate and phosphorylated intermediates. A new type of plastidic 2-oxoglutarate/malate transporter has been identified and represents the first carrier with 12 putative transmembrane domains, to be located in the inner envelope membrane. The plastidic ATP/ADP transporter also contains 12 putative transmembrane domains and possesses striking structural similarity to ATP/ADP transporters found in intracellular, human pathogenic bacteria.  (+info)

Identification of the pore-forming region of the outer chloroplast envelope protein OEP16. (2/207)

The chloroplast outer envelope protein OEP16 forms a cation-selective high conductance channel with permeability to amines and amino acids. The region of OEP16 directly involved in channel formation has been identified by electrophysiological analysis of a selection of reconstituted OEP16 mutants. Because analysis of these mutants depended on the use of recombinant protein, we evaluated the electrophysiological properties of OEP16 isolated directly from pea chloroplasts and of the recombinant protein produced in Escherichia coli. The results show that the basic properties like conductance, selectivity, and open probability of the channel formed by native pea OEP16 are comparable with the channel activity formed by the recombinant source of the protein. Following electrophysiological analysis of OEP16 mutants we found that point mutations and insertion of additional amino acid residues in the region of the putative helix 1 (Glu(73) to Val(91)) did not change the properties of the OEP16 channel. The only exception was a Cys(71)-->Ser mutation, which led to a loss of the CuCl(2) sensitivity of the channel. Analysis of N- and C-terminal deletion mutants of OEP16 and mutants containing defined shuffled domains indicated that the minimal continuous region of OEP16, which is able to form a channel in liposomes, lies in the first half of the protein between amino acid residues 21 and 93.  (+info)

Ontogenetic changes of potato plants during acclimation to elevated carbon dioxide. (3/207)

Transgenic potato plants (Solanum tuberosum cv. Desiree) with an antisense repression of the chloroplastic triosephosphate translocator were compared with wild-type plants. Plants were grown in chambers with either an atmosphere with ambient (400 mu bar) or elevated (1000 mu bar) CO2. After 7 weeks, the rate of CO2 assimilation between wild-type and transgenic plants in both CO2 concentrations was identical, but the tuber yield of both plant lines was increased by about 30%, when grown in elevated CO2. One explanation is that plants respond to the elevated CO2 only at a certain growth stage. Therefore, growth of wild-type plants was analysed between the second and the seventh week. Relative growth rate and CO2 assimilation were stimulated in elevated CO2 only in the second and the third weeks. During this period, the carbohydrate content of leaves grown with elevated CO2 was lower than that of leaves grown with ambient CO2. In plants grown in elevated CO2, the rate of CO2 assimilation started to decline after 5 weeks, and accumulation of carbohydrates began after 7 weeks. From this observation it was concluded that acclimation of potato plants to elevated CO2 is the result of accelerated development rather than of carbohydrate accumulation causing down-regulation of photosynthesis. For a detailed analysis for the cause of the stimulation of growth after 2 weeks, the contents of phosphorylated intermediates of wild-type plants and transgenics were measured. Stimulation of CO2 assimilation was accompanied by changes in the contents of phosphorylated intermediates, resulting in an increase in the amount of dihydroxyacetone phosphate, the metabolite which is exported from the chloroplast into the cytosol. An increase of dihydroxyacetone phosphate was found in wild-type plants in elevated CO2 when compared with ambient CO2 and in triosephosphate translocator antisense plants in ambient CO2, but not in the transgenic plants when grown in elevated CO2. These plants were not able to increase dihydroxyacetone phosphate further to cope with the increased CO2 supply. From these changes in phosphorylated intermediates in wild-type and transgenic plants it was concluded that starch and sucrose synthesis pathways can replace each other only at moderate carbon flux rates.  (+info)

Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts. (4/207)

In order to ascertain whether there is one site for the import of precursor proteins into chloroplasts or whether different precursor proteins are imported via different import machineries, chloroplasts were incubated with large quantities of the precursor of the 33 kDa subunit of the oxygen-evolving complex (pOE33) or the precursor of the light-harvesting chlorophyll a/b-binding protein (pLHCP) and tested for their ability to import a wide range of other chloroplast precursor proteins. Both pOE33 and pLHCP competed for import into chloroplasts with precursors of the stromally-targeted small subunit of Rubisco (pSSu), ferredoxin NADP(+) reductase (pFNR) and porphobilinogen deaminase; the thylakoid membrane proteins LHCP and the Rieske iron-sulphur protein (pRieske protein); ferrochelatase and the gamma subunit of the ATP synthase (which are both associated with the thylakoid membrane); the thylakoid lumenal protein plastocyanin and the phosphate translocator, an integral membrane protein of the inner envelope. The concentrations of pOE33 or pLHCP required to cause half-maximal inhibition of import ranged between 0.2 and 4.9 microM. These results indicate that all of these proteins are imported into the chloroplast by a common import machinery. Incubation of chloroplasts with pOE33 inhibited the formation of early import intermediates of pSSu, pFNR and pRieske protein.  (+info)

The effect of amino acid-modifying reagents on chloroplast protein import and the formation of early import intermediates. (5/207)

In order to identify functionally important amino acid residues in the chloroplast protein import machinery, chloroplasts were preincubated with amino-acid-modifying reagents and then allowed to import or form early import intermediates with precursor proteins. Incubation of chloroplasts with N-ethyl maleimide, diethyl pyrocarbonate, phenylglyoxal, 4,4'-di-isothiocyanatostilbene 2,2'-disulphonic acid (DIDS), dicyclohexylcarbodiimide (DCCD), and 1-ethyl- 3-dimethylaminopropylcarbodiimide (EDC) inhibited both import and formation of early import intermediates with precursor proteins by chloroplasts. This suggests that one or more of the binding components of the chloroplast protein import machinery contains functionally important solvent-exposed cysteine, histidine, arginine, and aspartate/glutamate residues, as well as functionally important lysine and aspartate/ glutamate residues in a hydrophobic environment.  (+info)

Involvement of a site-specific trans-acting factor and a common RNA-binding protein in the editing of chloroplast mRNAs: development of a chloroplast in vitro RNA editing system. (6/207)

RNA editing in higher plant chloroplasts involves C-->U conversion at approximately 30 specific sites. An in vitro system supporting accurate editing has been developed from tobacco chloroplasts. Mutational analysis of substrate mRNAs derived from tobacco chloroplast psbL and ndhB mRNAs confirmed the participation of cis-acting elements that had previously been identified in vivo. Competition analysis revealed the existence of site-specific trans-acting factors interacting with the corresponding upstream cis-elements. A chloroplast protein of 25 kDa was found to be specifically associated with the cis-element involved in psbL mRNA editing. Immunological analyses revealed that an additional factor, the chloroplast RNA-binding protein cp31, is also required for RNA editing at multiple sites. This combination of site-specific and common RNA-binding proteins recognizes editing sites in chloroplasts.  (+info)

Transcriptional repression and developmental functions of the atypical vertebrate GATA protein TRPS1. (7/207)

Known vertebrate GATA proteins contain two zinc fingers and are required in development, whereas invertebrates express a class of essential proteins containing one GATA-type zinc finger. We isolated the gene encoding TRPS1, a vertebrate protein with a single GATA-type zinc finger. TRPS1 is highly conserved between Xenopus and mammals, and the human gene is implicated in dominantly inherited tricho-rhino-phalangeal (TRP) syndromes. TRPS1 is a nuclear protein that binds GATA sequences but fails to transactivate a GATA-dependent reporter. Instead, TRPS1 potently and specifically represses transcriptional activation mediated by other GATA factors. Repression does not occur from competition for DNA binding and depends on a C-terminal region related to repressive domains found in Ikaros proteins. During mouse development, TRPS1 expression is prominent in sites showing pathology in TRP syndromes, which are thought to result from TRPS1 haploinsufficiency. We show instead that truncating mutations identified in patients encode dominant inhibitors of wild-type TRPS1 function, suggesting an alternative mechanism for the disease. TRPS1 is the first example of a GATA protein with intrinsic transcriptional repression activity and possibly a negative regulator of GATA-dependent processes in vertebrate development.  (+info)

Identification of an RNA-protein complex involved in chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii. (8/207)

In Chlamydomonas reinhardtii, the psaA mRNA is assembled by a process involving trans-splicing of separate transcripts, encoded at three separate loci of the chloroplast genome. At least 14 nuclear loci and one chloroplast gene, tscA, are needed for this process. We have cloned Raa3, the first nuclear gene implicated in the splicing of intron 1. The predicted sequence of Raa3 consists of 1783 amino acids and shares a small region of homology with pyridoxamine 5'-phosphate oxidases. Raa3 is present in the soluble fraction of the chloroplast and is part of a large 1700 kDa complex, which also contains tscA RNA and the first psaA exon transcript. These partners, in association with other factors, form a chloroplast RNP particle that is required for the splicing of the first intron of psaA and which may be the counterpart of eukaryotic snRNPs involved in nuclear splicing.  (+info)

Chloroplasts are specialized organelles found in the cells of green plants, algae, and some protists. They are responsible for carrying out photosynthesis, which is the process by which these organisms convert light energy from the sun into chemical energy in the form of organic compounds, such as glucose.

Chloroplasts contain the pigment chlorophyll, which absorbs light energy from the sun. They also contain a system of membranes and enzymes that convert carbon dioxide and water into glucose and oxygen through a series of chemical reactions known as the Calvin cycle. This process not only provides energy for the organism but also releases oxygen as a byproduct, which is essential for the survival of most life forms on Earth.

Chloroplasts are believed to have originated from ancient cyanobacteria that were engulfed by early eukaryotic cells and eventually became integrated into their host's cellular machinery through a process called endosymbiosis. Over time, chloroplasts evolved to become an essential component of plant and algal cells, contributing to their ability to carry out photosynthesis and thrive in a wide range of environments.

Chloroplasts are organelles found in the cells of plants, algae, and some protists. They are responsible for carrying out photosynthesis, which is the process by which these organisms convert light energy into chemical energy. Chloroplast proteins are the various proteins that are located within the chloroplasts and play a crucial role in the process of photosynthesis.

Chloroplasts contain several types of proteins, including:

1. Structural proteins: These proteins help to maintain the structure and integrity of the chloroplast.
2. Photosynthetic proteins: These are involved in capturing light energy and converting it into chemical energy during photosynthesis. They include proteins such as photosystem I, photosystem II, cytochrome b6f complex, and ATP synthase.
3. Regulatory proteins: These proteins help to regulate the various processes that occur within the chloroplast, including gene expression, protein synthesis, and energy metabolism.
4. Metabolic proteins: These proteins are involved in various metabolic pathways within the chloroplast, such as carbon fixation, amino acid synthesis, and lipid metabolism.
5. Protective proteins: These proteins help to protect the chloroplast from damage caused by reactive oxygen species (ROS) that are produced during photosynthesis.

Overall, chloroplast proteins play a critical role in maintaining the health and function of chloroplasts, and by extension, the overall health and survival of plants and other organisms that contain them.

"Plant proteins" refer to the proteins that are derived from plant sources. These can include proteins from legumes such as beans, lentils, and peas, as well as proteins from grains like wheat, rice, and corn. Other sources of plant proteins include nuts, seeds, and vegetables.

Plant proteins are made up of individual amino acids, which are the building blocks of protein. While animal-based proteins typically contain all of the essential amino acids that the body needs to function properly, many plant-based proteins may be lacking in one or more of these essential amino acids. However, by consuming a variety of plant-based foods throughout the day, it is possible to get all of the essential amino acids that the body needs from plant sources alone.

Plant proteins are often lower in calories and saturated fat than animal proteins, making them a popular choice for those following a vegetarian or vegan diet, as well as those looking to maintain a healthy weight or reduce their risk of chronic diseases such as heart disease and cancer. Additionally, plant proteins have been shown to have a number of health benefits, including improving gut health, reducing inflammation, and supporting muscle growth and repair.

I'm sorry for any confusion, but "peas" is not a term typically used in medical definitions. Peas are a type of legume that is commonly consumed as a vegetable. They are rich in nutrients such as protein, fiber, vitamin C, and vitamin K. If you have any questions about the health benefits or potential risks of consuming peas, I would be happy to try to help with that.

Chloroplast DNA (cpDNA) refers to the genetic material present in the chloroplasts, which are organelles found in the cells of photosynthetic organisms such as plants, algae, and some bacteria. Chloroplasts are responsible for capturing sunlight energy and converting it into chemical energy through the process of photosynthesis.

Chloroplast DNA is circular and contains a small number of genes compared to the nuclear genome. It encodes for some of the essential components required for chloroplast function, including proteins involved in photosynthesis, transcription, and translation. The majority of chloroplast proteins are encoded by the nuclear genome and are imported into the chloroplast after being synthesized in the cytoplasm.

Chloroplast DNA is inherited maternally in most plants, meaning that it is passed down from the maternal parent to their offspring through the egg cell. This mode of inheritance has been used in plant breeding and genetic engineering to introduce desirable traits into crops.

I'm happy to help! However, I believe there might be a slight confusion in your question. RNA and chloroplasts are two different biological concepts. Let me clarify:

1. RNA (Ribonucleic Acid): It is a type of nucleic acid that plays several crucial roles in the process of translation, decoding the genetic information stored in DNA into proteins. There are three main types of RNA: messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA).

2. Chloroplasts: They are specialized organelles found in the cells of green plants, algae, and some protists. Chloroplasts are responsible for capturing sunlight's energy and converting it into chemical energy through photosynthesis, which is used to produce glucose and oxygen.

There is no medical definition directly related to 'RNA, chloroplast' as they are separate concepts in biology. However, RNA does play a role in the expression of genes found within the chloroplast genome during photosynthesis. If you have any further questions or need more information about either concept, please let me know!

Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a crucial enzyme in the Calvin cycle, which is a process that plants use to convert carbon dioxide into glucose during photosynthesis. RuBisCO catalyzes the reaction between ribulose-1,5-bisphosphate and carbon dioxide, resulting in the formation of two molecules of 3-phosphoglycerate, which can then be converted into glucose.

RuBisCO is considered to be the most abundant enzyme on Earth, making up as much as 50% of the soluble protein found in leaves. It is a large and complex enzyme, consisting of eight small subunits and eight large subunits that are arranged in a barrel-shaped structure. The active site of the enzyme, where the reaction between ribulose-1,5-bisphosphate and carbon dioxide takes place, is located at the interface between two large subunits.

RuBisCO also has a secondary function as an oxygenase, which can lead to the production of glycolate, a toxic compound for plants. This reaction occurs when the enzyme binds with oxygen instead of carbon dioxide and is more prevalent in environments with low carbon dioxide concentrations and high oxygen concentrations. The glycolate produced during this process needs to be recycled through a series of reactions known as photorespiration, which can result in significant energy loss for the plant.

Thylakoids are membrane-bound structures located in the chloroplasts of plant cells and some protists. They are the site of the light-dependent reactions of photosynthesis, where light energy is converted into chemical energy in the form of ATP (adenosine triphosphate) and NADPH (nicotinamide adenine dinucleotide phosphate). Thylakoids have a characteristic stacked or disc-like structure, called grana, and are interconnected by unstacked regions called stroma lamellae. The arrangement of thylakoids in grana increases the surface area for absorption of light energy, allowing for more efficient photosynthesis.

A chloroplast genome is the entire genetic material that is present in the chloroplasts, which are organelles found in plant cells and some protists. The chloroplast genome is circular in shape and contains about 120-160 kilobases (kb) of DNA. It encodes for a small number of proteins, ribosomal RNAs, and transfer RNAs that are required for the function of the chloroplasts, particularly in photosynthesis. The chloroplast genome is usually inherited maternally, meaning it is passed down from the mother to her offspring.

The chloroplast genome is relatively simple compared to the nuclear genome, which contains many more genes and regulatory elements. However, most of the proteins required for chloroplast function are actually encoded in the nucleus and imported into the chloroplasts. The study of chloroplast genomes can provide insights into the evolutionary history of plants and their photosynthetic ancestors.

Chlorophyll is a green pigment found in the chloroplasts of photosynthetic plants, algae, and some bacteria. It plays an essential role in light-dependent reactions of photosynthesis by absorbing light energy, primarily from the blue and red parts of the electromagnetic spectrum, and converting it into chemical energy to fuel the synthesis of carbohydrates from carbon dioxide and water. The structure of chlorophyll includes a porphyrin ring, which binds a central magnesium ion, and a long phytol tail. There are several types of chlorophyll, including chlorophyll a and chlorophyll b, which have distinct absorption spectra and slightly different structures. Chlorophyll is crucial for the process of photosynthesis, enabling the conversion of sunlight into chemical energy and the release of oxygen as a byproduct.

Photosynthesis is not strictly a medical term, but it is a fundamental biological process with significant implications for medicine, particularly in understanding energy production in cells and the role of oxygen in sustaining life. Here's a general biological definition:

Photosynthesis is a process by which plants, algae, and some bacteria convert light energy, usually from the sun, into chemical energy in the form of organic compounds, such as glucose (or sugar), using water and carbon dioxide. This process primarily takes place in the chloroplasts of plant cells, specifically in structures called thylakoids. The overall reaction can be summarized as:

6 CO2 + 6 H2O + light energy → C6H12O6 + 6 O2

In this equation, carbon dioxide (CO2) and water (H2O) are the reactants, while glucose (C6H12O6) and oxygen (O2) are the products. Photosynthesis has two main stages: the light-dependent reactions and the light-independent reactions (Calvin cycle). The light-dependent reactions occur in the thylakoid membrane and involve the conversion of light energy into ATP and NADPH, which are used to power the Calvin cycle. The Calvin cycle takes place in the stroma of chloroplasts and involves the synthesis of glucose from CO2 and water using the ATP and NADPH generated during the light-dependent reactions.

Understanding photosynthesis is crucial for understanding various biological processes, including cellular respiration, plant metabolism, and the global carbon cycle. Additionally, research into artificial photosynthesis has potential applications in renewable energy production and environmental remediation.

'Arabidopsis' is a genus of small flowering plants that are part of the mustard family (Brassicaceae). The most commonly studied species within this genus is 'Arabidopsis thaliana', which is often used as a model organism in plant biology and genetics research. This plant is native to Eurasia and Africa, and it has a small genome that has been fully sequenced. It is known for its short life cycle, self-fertilization, and ease of growth, making it an ideal subject for studying various aspects of plant biology, including development, metabolism, and response to environmental stresses.

Arabidopsis proteins refer to the proteins that are encoded by the genes in the Arabidopsis thaliana plant, which is a model organism commonly used in plant biology research. This small flowering plant has a compact genome and a short life cycle, making it an ideal subject for studying various biological processes in plants.

Arabidopsis proteins play crucial roles in many cellular functions, such as metabolism, signaling, regulation of gene expression, response to environmental stresses, and developmental processes. Research on Arabidopsis proteins has contributed significantly to our understanding of plant biology and has provided valuable insights into the molecular mechanisms underlying various agronomic traits.

Some examples of Arabidopsis proteins include transcription factors, kinases, phosphatases, receptors, enzymes, and structural proteins. These proteins can be studied using a variety of techniques, such as biochemical assays, protein-protein interaction studies, and genetic approaches, to understand their functions and regulatory mechanisms in plants.

Chlamydomonas is a genus of single-celled, green algae that are widely found in freshwater and marine environments. These microorganisms are characterized by their oval or spherical shape, and each cell contains a single, large chloroplast used for photosynthesis. They also have two flagella, which are hair-like structures that enable them to move through their aquatic habitats. Chlamydomonas species are often used in scientific research due to their simple cell structure and ease of cultivation in the lab.

Chlamydomonas reinhardtii is a species of single-celled, freshwater green algae. It is commonly used as a model organism in scientific research due to its simple unicellular structure and the ease with which it can be genetically manipulated. C. reinhardtii has a single, large chloroplast that contains both photosynthetic pigments and a nucleomorph, a remnant of a secondary endosymbiotic event where another alga was engulfed by an ancestral eukaryote. This species is capable of both phototactic and photophobic responses, allowing it to move towards or away from light sources. Additionally, C. reinhardtii has two flagella for locomotion, making it a popular subject for ciliary and flagellar research. It undergoes closed mitosis within its single, diploid nucleus, which is surrounded by a cell wall composed of glycoproteins. The genome of C. reinhardtii has been fully sequenced, providing valuable insights into the molecular mechanisms underlying photosynthesis, flagellar assembly, and other fundamental biological processes.

I apologize for any confusion, but "plants" is not a term that has a medical definition. The term "plants" refers to a large and diverse group of organisms that obtain their energy through photosynthesis, which is the process of converting sunlight into chemical energy. Plants are typically characterized by having cells with cell walls containing cellulose, chloroplasts containing the pigment chlorophyll, and the ability to synthesize their own food through photosynthesis.

In a medical or biological context, you might be thinking of "plant-based" or "phytomedicine," which refer to the use of plants or plant extracts as a form of medicine or treatment. Phytomedicines have been used for thousands of years in many traditional systems of medicine, and some plant-derived compounds have been found to have therapeutic benefits in modern medicine as well. However, "plants" itself does not have a medical definition.

'Euglena gracilis' is a species of unicellular flagellate belonging to the genus Euglena. It is a common freshwater organism, characterized by its elongated, flexible shape and distinct eyespot that allows it to move towards light sources. 'Euglena gracilis' contains chloroplasts for photosynthesis but can also consume other organic matter through phagocytosis, making it a facultative autotroph. It is often used as a model organism in scientific research due to its unique combination of features from both plant and animal kingdoms.

Plastids are membrane-bound organelles found in the cells of plants and algae. They are responsible for various cellular functions, including photosynthesis, storage of starch, lipids, and proteins, and the production of pigments that give plants their color. The most common types of plastids are chloroplasts (which contain chlorophyll and are involved in photosynthesis), chromoplasts (which contain pigments such as carotenoids and are responsible for the yellow, orange, and red colors of fruits and flowers), and leucoplasts (which do not contain pigments and serve mainly as storage organelles). Plastids have their own DNA and can replicate themselves within the cell.

Chloroplast thioredoxins are small, heat-stable proteins located in the chloroplasts of plant cells. They play a crucial role in regulating various metabolic processes in the chloroplast, particularly those related to photosynthesis. Thioredoxins function as electron carriers and reduce disulfide bonds in target proteins, thereby activating or deactivating their enzymatic activity.

Chloroplast thioredoxins are reduced by ferredoxin-thioredoxin reductase using electrons supplied by photosystem I during light reactions of photosynthesis. This reduction process enables chloroplast thioredoxins to regulate the activity of various enzymes involved in carbon fixation, such as Rubisco (Ribulose-1,5-bisphosphate carboxylase/oxygenase), and other metabolic processes like protein folding and degradation.

There are multiple isoforms of chloroplast thioredoxins (trx), including TrxA, TrxB, TrxC, and TrxD, each with distinct roles in regulating specific target proteins and cellular processes. The regulation of chloroplast thioredoxins and their targets is critical for maintaining optimal photosynthetic efficiency and adapting to changing environmental conditions.

In the context of medical terminology, "light" doesn't have a specific or standardized definition on its own. However, it can be used in various medical terms and phrases. For example, it could refer to:

1. Visible light: The range of electromagnetic radiation that can be detected by the human eye, typically between wavelengths of 400-700 nanometers. This is relevant in fields such as ophthalmology and optometry.
2. Therapeutic use of light: In some therapies, light is used to treat certain conditions. An example is phototherapy, which uses various wavelengths of ultraviolet (UV) or visible light for conditions like newborn jaundice, skin disorders, or seasonal affective disorder.
3. Light anesthesia: A state of reduced consciousness in which the patient remains responsive to verbal commands and physical stimulation. This is different from general anesthesia where the patient is completely unconscious.
4. Pain relief using light: Certain devices like transcutaneous electrical nerve stimulation (TENS) units have a 'light' setting, indicating lower intensity or frequency of electrical impulses used for pain management.

Without more context, it's hard to provide a precise medical definition of 'light'.

'Euglena' is a genus of unicellular flagellate protists that are typically characterized by their oval-shaped bodies, long whip-like tail (flagellum), and eyespot (stigma) which helps them to move towards light. They are commonly found in freshwater environments and can also be found in soil and brackish water. Some species of Euglena have the ability to photosynthesize, while others obtain their nutrition through heterotrophy (consuming other organisms or organic matter). The term 'Euglena' is derived from the Greek word 'euglenes', which means "well-shaped" or "true-eyed". Medical professionals and researchers may study Euglena as part of broader research into protists, microbiology, or ecology.

Photosystem II Protein Complex is a crucial component of the photosynthetic apparatus in plants, algae, and cyanobacteria. It is a multi-subunit protein complex located in the thylakoid membrane of the chloroplasts. Photosystem II plays a vital role in light-dependent reactions of photosynthesis, where it absorbs sunlight and uses its energy to drive the oxidation of water molecules into oxygen, electrons, and protons.

The protein complex consists of several subunits, including the D1 and D2 proteins, which form the reaction center, and several antenna proteins that capture light energy and transfer it to the reaction center. Photosystem II also contains various cofactors, such as pigments (chlorophylls and carotenoids), redox-active metal ions (manganese and calcium), and quinones, which facilitate the charge separation and electron transfer processes during photosynthesis.

Photosystem II Protein Complex is responsible for the initial charge separation event in photosynthesis, which sets off a series of redox reactions that ultimately lead to the reduction of NADP+ to NADPH and the synthesis of ATP, providing energy for the carbon fixation reactions in the Calvin cycle. Additionally, Photosystem II Protein Complex is involved in oxygen evolution, contributing to the Earth's atmosphere's oxygen levels and making it an essential component of global carbon fixation and oxygen production.

Algal proteins are a type of protein that are derived from algae, which are simple, plant-like organisms that live in water. These proteins can be extracted and isolated from the algae through various processing methods and can then be used as a source of nutrition for both humans and animals.

Algal proteins are considered to be a complete protein source because they contain all of the essential amino acids that the body cannot produce on its own. They are also rich in other nutrients, such as vitamins, minerals, and antioxidants. Some species of algae, such as spirulina and chlorella, have particularly high protein contents, making them a popular choice for use in dietary supplements and functional foods.

In addition to their nutritional benefits, algal proteins are also being studied for their potential therapeutic uses. For example, some research suggests that they may have anti-inflammatory, antioxidant, and immune-boosting properties. However, more research is needed to confirm these potential health benefits and to determine the optimal dosages and methods of use.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

"Spinacia oleracea" is the scientific name for a plant species, not a medical term. It is commonly known as spinach, a leafy green vegetable. While spinach has many health benefits and is often recommended as part of a balanced diet, it does not have a specific medical definition.

Spinach is rich in various nutrients such as iron, calcium, vitamin A, vitamin C, and folic acid. It can contribute to overall health, support immune function, and provide antioxidant benefits. However, it is important to note that 'Spinacia oleracea' itself does not have a medical definition.

Medicinal plants are defined as those plants that contain naturally occurring chemical compounds which can be used for therapeutic purposes, either directly or indirectly. These plants have been used for centuries in various traditional systems of medicine, such as Ayurveda, Chinese medicine, and Native American medicine, to prevent or treat various health conditions.

Medicinal plants contain a wide variety of bioactive compounds, including alkaloids, flavonoids, tannins, terpenes, and saponins, among others. These compounds have been found to possess various pharmacological properties, such as anti-inflammatory, analgesic, antimicrobial, antioxidant, and anticancer activities.

Medicinal plants can be used in various forms, including whole plant material, extracts, essential oils, and isolated compounds. They can be administered through different routes, such as oral, topical, or respiratory, depending on the desired therapeutic effect.

It is important to note that while medicinal plants have been used safely and effectively for centuries, they should be used with caution and under the guidance of a healthcare professional. Some medicinal plants can interact with prescription medications or have adverse effects if used inappropriately.

Photosynthetic Reaction Center (RC) Complex Proteins are specialized protein-pigment structures that play a crucial role in the primary process of light-driven electron transport during photosynthesis. They are present in the thylakoid membranes of cyanobacteria, algae, and higher plants.

The Photosynthetic Reaction Center Complex Proteins are composed of two major components: the light-harvesting complex (LHC) and the reaction center (RC). The LHC contains antenna pigments like chlorophylls and carotenoids that absorb sunlight and transfer the excitation energy to the RC. The RC is a multi-subunit protein complex containing cofactors such as bacteriochlorophyll, pheophytin, quinones, and iron-sulfur clusters.

When a photon of light is absorbed by the antenna pigments in the LHC, the energy is transferred to the RC, where it initiates a charge separation event. This results in the transfer of an electron from a donor molecule to an acceptor molecule, creating a flow of electrical charge and generating a transmembrane electrochemical gradient. The energy stored in this gradient is then used to synthesize ATP and reduce NADP+, which are essential for carbon fixation and other metabolic processes in the cell.

In summary, Photosynthetic Reaction Center Complex Proteins are specialized protein structures involved in capturing light energy and converting it into chemical energy during photosynthesis, ultimately driving the synthesis of ATP and NADPH for use in carbon fixation and other metabolic processes.

I believe there may be a slight misunderstanding in your question. "Plant leaves" are not a medical term, but rather a general biological term referring to a specific organ found in plants.

Leaves are organs that are typically flat and broad, and they are the primary site of photosynthesis in most plants. They are usually green due to the presence of chlorophyll, which is essential for capturing sunlight and converting it into chemical energy through photosynthesis.

While leaves do not have a direct medical definition, understanding their structure and function can be important in various medical fields, such as pharmacognosy (the study of medicinal plants) or environmental health. For example, certain plant leaves may contain bioactive compounds that have therapeutic potential, while others may produce allergens or toxins that can impact human health.

Light-harvesting protein complexes are specialized structures in photosynthetic organisms, such as plants, algae, and some bacteria, that capture and transfer light energy to the reaction centers where the initial chemical reactions of photosynthesis occur. These complexes consist of proteins and pigments (primarily chlorophylls and carotenoids) arranged in a way that allows them to absorb light most efficiently. The absorbed light energy is then converted into electrical charges, which are transferred to the reaction centers for further chemical reactions leading to the production of organic compounds and oxygen. The light-harvesting protein complexes play a crucial role in initiating the process of photosynthesis and optimizing its efficiency by capturing and distributing light energy.

Protein precursors, also known as proproteins or prohormones, are inactive forms of proteins that undergo post-translational modification to become active. These modifications typically include cleavage of the precursor protein by specific enzymes, resulting in the release of the active protein. This process allows for the regulation and control of protein activity within the body. Protein precursors can be found in various biological processes, including the endocrine system where they serve as inactive hormones that can be converted into their active forms when needed.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Fabaceae is the scientific name for a family of flowering plants commonly known as the legume, pea, or bean family. This family includes a wide variety of plants that are important economically, agriculturally, and ecologically. Many members of Fabaceae have compound leaves and produce fruits that are legumes, which are long, thin pods that contain seeds. Some well-known examples of plants in this family include beans, peas, lentils, peanuts, clover, and alfalfa.

In addition to their importance as food crops, many Fabaceae species have the ability to fix nitrogen from the atmosphere into the soil through a symbiotic relationship with bacteria that live in nodules on their roots. This makes them valuable for improving soil fertility and is one reason why they are often used in crop rotation and as cover crops.

It's worth noting that Fabaceae is sometimes still referred to by its older scientific name, Leguminosae.

Gene expression regulation in plants refers to the processes that control the production of proteins and RNA from the genes present in the plant's DNA. This regulation is crucial for normal growth, development, and response to environmental stimuli in plants. It can occur at various levels, including transcription (the first step in gene expression, where the DNA sequence is copied into RNA), RNA processing (such as alternative splicing, which generates different mRNA molecules from a single gene), translation (where the information in the mRNA is used to produce a protein), and post-translational modification (where proteins are chemically modified after they have been synthesized).

In plants, gene expression regulation can be influenced by various factors such as hormones, light, temperature, and stress. Plants use complex networks of transcription factors, chromatin remodeling complexes, and small RNAs to regulate gene expression in response to these signals. Understanding the mechanisms of gene expression regulation in plants is important for basic research, as well as for developing crops with improved traits such as increased yield, stress tolerance, and disease resistance.

Genetically modified plants (GMPs) are plants that have had their DNA altered through genetic engineering techniques to exhibit desired traits. These modifications can be made to enhance certain characteristics such as increased resistance to pests, improved tolerance to environmental stresses like drought or salinity, or enhanced nutritional content. The process often involves introducing genes from other organisms, such as bacteria or viruses, into the plant's genome. Examples of GMPs include Bt cotton, which has a gene from the bacterium Bacillus thuringiensis that makes it resistant to certain pests, and golden rice, which is engineered to contain higher levels of beta-carotene, a precursor to vitamin A. It's important to note that genetically modified plants are subject to rigorous testing and regulation to ensure their safety for human consumption and environmental impact before they are approved for commercial use.

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

Chloroplast genes refer to the genetic material present within chloroplasts, which are specialized organelles in plant and algal cells that conduct photosynthesis. Chloroplasts have their own DNA, separate from the nuclear DNA of the cell, and can replicate independently. The chloroplast genome is relatively small and contains codes for some of the essential proteins required for photosynthesis and chloroplast function.

The chloroplast genome typically includes genes for components of the photosystems, such as Psa and Psb genes that encode for subunits of Photosystem I and II respectively, as well as genes for the large and small ribosomal RNAs (rRNA) and transfer RNAs (tRNA) required for protein synthesis within the chloroplast. However, many chloroplast proteins are actually encoded by nuclear genes and are imported into the chloroplast after their synthesis in the cytoplasm.

It is believed that chloroplasts originated from ancient photosynthetic bacteria through endosymbiosis, where the bacterial cells were engulfed by a eukaryotic cell and eventually became permanent organelles within the host cell. Over time, much of the bacterial genome was either lost or transferred to the host cell's nucleus, resulting in the modern-day chloroplast genome.

Intracellular membranes refer to the membrane structures that exist within a eukaryotic cell (excluding bacteria and archaea, which are prokaryotic and do not have intracellular membranes). These membranes compartmentalize the cell, creating distinct organelles or functional regions with specific roles in various cellular processes.

Major types of intracellular membranes include:

1. Nuclear membrane (nuclear envelope): A double-membraned structure that surrounds and protects the genetic material within the nucleus. It consists of an outer and inner membrane, perforated by nuclear pores that regulate the transport of molecules between the nucleus and cytoplasm.
2. Endoplasmic reticulum (ER): An extensive network of interconnected tubules and sacs that serve as a major site for protein folding, modification, and lipid synthesis. The ER has two types: rough ER (with ribosomes on its surface) and smooth ER (without ribosomes).
3. Golgi apparatus/Golgi complex: A series of stacked membrane-bound compartments that process, sort, and modify proteins and lipids before they are transported to their final destinations within the cell or secreted out of the cell.
4. Lysosomes: Membrane-bound organelles containing hydrolytic enzymes for breaking down various biomolecules (proteins, carbohydrates, lipids, and nucleic acids) in the process called autophagy or from outside the cell via endocytosis.
5. Peroxisomes: Single-membrane organelles involved in various metabolic processes, such as fatty acid oxidation and detoxification of harmful substances like hydrogen peroxide.
6. Vacuoles: Membrane-bound compartments that store and transport various molecules, including nutrients, waste products, and enzymes. Plant cells have a large central vacuole for maintaining turgor pressure and storing metabolites.
7. Mitochondria: Double-membraned organelles responsible for generating energy (ATP) through oxidative phosphorylation and other metabolic processes, such as the citric acid cycle and fatty acid synthesis.
8. Chloroplasts: Double-membraned organelles found in plant cells that convert light energy into chemical energy during photosynthesis, producing oxygen and organic compounds (glucose) from carbon dioxide and water.
9. Endoplasmic reticulum (ER): A network of interconnected membrane-bound tubules involved in protein folding, modification, and transport; it is divided into two types: rough ER (with ribosomes on the surface) and smooth ER (without ribosomes).
10. Nucleus: Double-membraned organelle containing genetic material (DNA) and associated proteins involved in replication, transcription, RNA processing, and DNA repair. The nuclear membrane separates the nucleoplasm from the cytoplasm and contains nuclear pores for transporting molecules between the two compartments.

A gene in plants, like in other organisms, is a hereditary unit that carries genetic information from one generation to the next. It is a segment of DNA (deoxyribonucleic acid) that contains the instructions for the development and function of an organism. Genes in plants determine various traits such as flower color, plant height, resistance to diseases, and many others. They are responsible for encoding proteins and RNA molecules that play crucial roles in the growth, development, and reproduction of plants. Plant genes can be manipulated through traditional breeding methods or genetic engineering techniques to improve crop yield, enhance disease resistance, and increase nutritional value.

Tobacco is not a medical term, but it refers to the leaves of the plant Nicotiana tabacum that are dried and fermented before being used in a variety of ways. Medically speaking, tobacco is often referred to in the context of its health effects. According to the World Health Organization (WHO), "tobacco" can also refer to any product prepared from the leaf of the tobacco plant for smoking, sucking, chewing or snuffing.

Tobacco use is a major risk factor for a number of diseases, including cancer, heart disease, stroke, lung disease, and various other medical conditions. The smoke produced by burning tobacco contains thousands of chemicals, many of which are toxic and can cause serious health problems. Nicotine, one of the primary active constituents in tobacco, is highly addictive and can lead to dependence.

Ribonucleic acid (RNA) in plants refers to the long, single-stranded molecules that are essential for the translation of genetic information from deoxyribonucleic acid (DNA) into proteins. RNA is a nucleic acid, like DNA, and it is composed of a ribose sugar backbone with attached nitrogenous bases (adenine, uracil, guanine, and cytosine).

In plants, there are several types of RNA that play specific roles in the gene expression process:

1. Messenger RNA (mRNA): This type of RNA carries genetic information copied from DNA in the form of a sequence of three-base code units called codons. These codons specify the order of amino acids in a protein.
2. Transfer RNA (tRNA): tRNAs are small RNA molecules that serve as adaptors between the mRNA and the amino acids during protein synthesis. Each tRNA has a specific anticodon sequence that base-pairs with a complementary codon on the mRNA, and it carries a specific amino acid that corresponds to that codon.
3. Ribosomal RNA (rRNA): rRNAs are structural components of ribosomes, which are large macromolecular complexes where protein synthesis occurs. In plants, there are several types of rRNAs, including the 18S, 5.8S, and 25S/28S rRNAs, that form the core of the ribosome and help catalyze peptide bond formation during protein synthesis.
4. Small nuclear RNA (snRNA): These are small RNA molecules that play a role in RNA processing, such as splicing, where introns (non-coding sequences) are removed from pre-mRNA and exons (coding sequences) are joined together to form mature mRNAs.
5. MicroRNA (miRNA): These are small non-coding RNAs that regulate gene expression by binding to complementary sequences in target mRNAs, leading to their degradation or translation inhibition.

Overall, these different types of RNAs play crucial roles in various aspects of RNA metabolism, gene regulation, and protein synthesis in plants.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

I am not aware of a medical definition for the term "darkness." In general, darkness refers to the absence of light. It is not a term that is commonly used in the medical field, and it does not have a specific clinical meaning. If you have a question about a specific medical term or concept, I would be happy to try to help you understand it.

Chloroplast proton-translocating ATPases, also known as CF1-CF0 ATP synthase, are complex enzymes found in the thylakoid membrane of chloroplasts. They play a crucial role in the process of photosynthesis by converting the energy generated from sunlight into chemical energy in the form of ATP (adenosine triphosphate).

The CF1 portion of the enzyme is located on the stromal side of the thylakoid membrane and contains the catalytic sites for ATP synthesis. The CF0 portion, on the other hand, spans the membrane and contains a proton channel that allows for the movement of protons (H+) across the membrane.

The process of ATP synthesis is driven by a proton gradient that is established across the thylakoid membrane during the light-dependent reactions of photosynthesis. As protons flow through the CF0 channel, they drive the rotation of a subunit within the enzyme complex, which in turn triggers the conversion of ADP (adenosine diphosphate) and phosphate into ATP at the CF1 catalytic sites.

Overall, chloroplast proton-translocating ATPases are essential for the generation of ATP in plants and other photosynthetic organisms, and play a critical role in maintaining the energy balance of the cell.

'Zea mays' is the biological name for corn or maize, which is not typically considered a medical term. However, corn or maize can have medical relevance in certain contexts. For example, cornstarch is sometimes used as a diluent for medications and is also a component of some skin products. Corn oil may be found in topical ointments and creams. In addition, some people may have allergic reactions to corn or corn-derived products. But generally speaking, 'Zea mays' itself does not have a specific medical definition.

Protein biosynthesis is the process by which cells generate new proteins. It involves two major steps: transcription and translation. Transcription is the process of creating a complementary RNA copy of a sequence of DNA. This RNA copy, or messenger RNA (mRNA), carries the genetic information to the site of protein synthesis, the ribosome. During translation, the mRNA is read by transfer RNA (tRNA) molecules, which bring specific amino acids to the ribosome based on the sequence of nucleotides in the mRNA. The ribosome then links these amino acids together in the correct order to form a polypeptide chain, which may then fold into a functional protein. Protein biosynthesis is essential for the growth and maintenance of all living organisms.

Ferredoxins are iron-sulfur proteins that play a crucial role in electron transfer reactions in various biological systems, particularly in photosynthesis and nitrogen fixation. They contain one or more clusters of iron and sulfur atoms (known as the iron-sulfur cluster) that facilitate the movement of electrons between different molecules during metabolic processes.

Ferredoxins have a relatively simple structure, consisting of a polypeptide chain that binds to the iron-sulfur cluster. This simple structure allows ferredoxins to participate in a wide range of redox reactions and makes them versatile electron carriers in biological systems. They can accept electrons from various donors and transfer them to different acceptors, depending on the needs of the cell.

In photosynthesis, ferredoxins play a critical role in the light-dependent reactions by accepting electrons from photosystem I and transferring them to NADP+, forming NADPH. This reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) is then used in the Calvin cycle for carbon fixation and the production of glucose.

In nitrogen fixation, ferredoxins help transfer electrons to the nitrogenase enzyme complex, which reduces atmospheric nitrogen gas (N2) into ammonia (NH3), making it available for assimilation by plants and other organisms.

Overall, ferredoxins are essential components of many metabolic pathways, facilitating electron transfer and energy conversion in various biological systems.

Photosystem I Protein Complex, also known as PsaA/B-Protein or Photosystem I reaction center, is a large protein complex found in the thylakoid membrane of plant chloroplasts and cyanobacteria. It plays a crucial role in light-dependent reactions of photosynthesis, where it absorbs light energy and converts it into chemical energy in the form of NADPH.

The complex is composed of several subunits, including PsaA and PsaB, which are the core components that bind to chlorophyll a and bacteriochlorophyll a pigments. These pigments absorb light energy and transfer it to the reaction center, where it is used to drive the electron transport chain and generate a proton gradient across the membrane. This gradient is then used to produce ATP, which provides energy for the carbon fixation reactions in photosynthesis.

Photosystem I Protein Complex is also involved in cyclic electron flow, where electrons are recycled within the complex to generate additional ATP without producing NADPH. This process helps regulate the balance between ATP and NADPH production in the chloroplast and optimizes the efficiency of photosynthesis.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Phylogeny is the evolutionary history and relationship among biological entities, such as species or genes, based on their shared characteristics. In other words, it refers to the branching pattern of evolution that shows how various organisms have descended from a common ancestor over time. Phylogenetic analysis involves constructing a tree-like diagram called a phylogenetic tree, which depicts the inferred evolutionary relationships among organisms or genes based on molecular sequence data or other types of characters. This information is crucial for understanding the diversity and distribution of life on Earth, as well as for studying the emergence and spread of diseases.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Chlorophyta is a division of green algae, also known as green plants. This group includes a wide variety of simple, aquatic organisms that contain chlorophylls a and b, which gives them their characteristic green color. They are a diverse group, ranging from unicellular forms to complex multicellular seaweeds. Chlorophyta is a large and varied division with approximately 7,00

Protein sorting signals, also known as sorting motifs or sorting determinants, are specific sequences or domains within a protein that determine its intracellular trafficking and localization. These signals can be found in the amino acid sequence of a protein and are recognized by various sorting machinery such as receptors, coat proteins, and transport vesicles. They play a crucial role in directing newly synthesized proteins to their correct destinations within the cell, including the endoplasmic reticulum (ER), Golgi apparatus, lysosomes, plasma membrane, or extracellular space.

There are several types of protein sorting signals, such as:

1. Signal peptides: These are short sequences of amino acids found at the N-terminus of a protein that direct it to the ER for translocation across the membrane and subsequent processing in the secretory pathway.
2. Transmembrane domains: Hydrophobic regions within a protein that span the lipid bilayer, often serving as anchors to tether proteins to specific organelle membranes or the plasma membrane.
3. Glycosylphosphatidylinositol (GPI) anchors: These are post-translational modifications added to the C-terminus of a protein, allowing it to be attached to the outer leaflet of the plasma membrane.
4. Endoplasmic reticulum retrieval signals: KDEL or KKXX-like sequences found at the C-terminus of proteins that direct their retrieval from the Golgi apparatus back to the ER.
5. Lysosomal targeting signals: Sequences within a protein, such as mannose 6-phosphate (M6P) residues or tyrosine-based motifs, that facilitate its recognition and transport to lysosomes.
6. Nuclear localization signals (NLS): Short sequences of basic amino acids that direct a protein to the nuclear pore complex for import into the nucleus.
7. Nuclear export signals (NES): Sequences rich in leucine residues that facilitate the export of proteins from the nucleus to the cytoplasm.

These various targeting and localization signals help ensure that proteins are delivered to their proper destinations within the cell, allowing for the coordinated regulation of cellular processes and functions.

Photophosphorylation is the process by which ATP (adenosine triphosphate) is produced during photosynthesis, utilizing light energy to add a phosphate group to ADP (adenosine diphosphate). This process occurs in the chloroplasts of plant cells and cyanobacteria, in a series of steps that are catalyzed by several complexes of proteins. There are two types of photophosphorylation: cyclic and non-cyclic. Cyclic photophosphorylation involves the use of only one photosystem and results in the production of ATP, while non-cyclic photophosphorylation involves the use of two photosystems and leads to the production of both ATP and NADPH, as well as the reduction of NADP+ to NADPH. Overall, photophosphorylation plays a crucial role in providing energy for various metabolic processes in plant cells and is essential for life on Earth.

A phenotype is the physical or biochemical expression of an organism's genes, or the observable traits and characteristics resulting from the interaction of its genetic constitution (genotype) with environmental factors. These characteristics can include appearance, development, behavior, and resistance to disease, among others. Phenotypes can vary widely, even among individuals with identical genotypes, due to differences in environmental influences, gene expression, and genetic interactions.

The cell nucleus is a membrane-bound organelle found in the eukaryotic cells (cells with a true nucleus). It contains most of the cell's genetic material, organized as DNA molecules in complex with proteins, RNA molecules, and histones to form chromosomes.

The primary function of the cell nucleus is to regulate and control the activities of the cell, including growth, metabolism, protein synthesis, and reproduction. It also plays a crucial role in the process of mitosis (cell division) by separating and protecting the genetic material during this process. The nuclear membrane, or nuclear envelope, surrounding the nucleus is composed of two lipid bilayers with numerous pores that allow for the selective transport of molecules between the nucleoplasm (nucleus interior) and the cytoplasm (cell exterior).

The cell nucleus is a vital structure in eukaryotic cells, and its dysfunction can lead to various diseases, including cancer and genetic disorders.

Galactolipids are a type of glycolipid, which are lipids that contain a carbohydrate moiety. They are the most abundant lipids in plant chloroplasts and play important roles in membrane structure and function. The term "galactolipid" refers to lipids that contain one or more galactose molecules as their polar headgroup.

The two major types of galactolipids are monogalactosyldiacylglycerols (MGDGs) and digalactosyldiacylglycerols (DGDGs). MGDGs contain a single galactose molecule, while DGDGs contain two. These lipids are important components of the thylakoid membrane in chloroplasts, where they help to maintain the structural integrity and fluidity of the membrane, as well as facilitate the movement of proteins and other molecules within it.

In addition to their role in plant cells, galactolipids have also been found to be important in animal cells, particularly in the brain. They are a major component of myelin sheaths, which surround and insulate nerve fibers, allowing for efficient electrical signaling. Abnormalities in galactolipid metabolism have been linked to several neurological disorders, including multiple sclerosis and Krabbe disease.

A genetic complementation test is a laboratory procedure used in molecular genetics to determine whether two mutated genes can complement each other's function, indicating that they are located at different loci and represent separate alleles. This test involves introducing a normal or wild-type copy of one gene into a cell containing a mutant version of the same gene, and then observing whether the presence of the normal gene restores the normal function of the mutated gene. If the introduction of the normal gene results in the restoration of the normal phenotype, it suggests that the two genes are located at different loci and can complement each other's function. However, if the introduction of the normal gene does not restore the normal phenotype, it suggests that the two genes are located at the same locus and represent different alleles of the same gene. This test is commonly used to map genes and identify genetic interactions in a variety of organisms, including bacteria, yeast, and animals.

Molecular chaperones are a group of proteins that assist in the proper folding and assembly of other protein molecules, helping them achieve their native conformation. They play a crucial role in preventing protein misfolding and aggregation, which can lead to the formation of toxic species associated with various neurodegenerative diseases. Molecular chaperones are also involved in protein transport across membranes, degradation of misfolded proteins, and protection of cells under stress conditions. Their function is generally non-catalytic and ATP-dependent, and they often interact with their client proteins in a transient manner.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

Two-dimensional (2D) gel electrophoresis is a type of electrophoretic technique used in the separation and analysis of complex protein mixtures. This method combines two types of electrophoresis – isoelectric focusing (IEF) and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) – to separate proteins based on their unique physical and chemical properties in two dimensions.

In the first dimension, IEF separates proteins according to their isoelectric points (pI), which is the pH at which a protein carries no net electrical charge. The proteins are focused into narrow zones along a pH gradient established within a gel strip. In the second dimension, SDS-PAGE separates the proteins based on their molecular weights by applying an electric field perpendicular to the first dimension.

The separated proteins form distinct spots on the 2D gel, which can be visualized using various staining techniques. The resulting protein pattern provides valuable information about the composition and modifications of the protein mixture, enabling researchers to identify and compare different proteins in various samples. Two-dimensional gel electrophoresis is widely used in proteomics research, biomarker discovery, and quality control in protein production.

The cytochrome b6f complex is a protein complex in the thylakoid membrane of the chloroplasts in plants, algae, and cyanobacteria. It plays a crucial role in the light-dependent reactions of photosynthesis by facilitating the transfer of electrons from photosystem II to photosystem I.

The complex is composed of four subunits: cytochrome b6, subunit IV, and two Rieske iron-sulfur proteins. Cytochrome b6 is a heme protein that contains two heme groups, while subunit IV helps anchor the complex in the thylakoid membrane. The Rieske iron-sulfur proteins contain a 2Fe-2S cluster and are responsible for transferring electrons between cytochrome b6 and plastoquinone, a mobile electron carrier.

The cytochrome b6f complex functions in the Q-cycle, which is a mechanism that increases the efficiency of electron transfer and generates a proton gradient across the thylakoid membrane. This proton gradient drives the synthesis of ATP, an essential energy currency for the cell. Overall, the cytochrome b6f complex is a vital component of the photosynthetic machinery, enabling the conversion of light energy into chemical energy in the form of ATP and NADPH.

DNA, or deoxyribonucleic acid, is the genetic material present in the cells of all living organisms, including plants. In plants, DNA is located in the nucleus of a cell, as well as in chloroplasts and mitochondria. Plant DNA contains the instructions for the development, growth, and function of the plant, and is passed down from one generation to the next through the process of reproduction.

The structure of DNA is a double helix, formed by two strands of nucleotides that are linked together by hydrogen bonds. Each nucleotide contains a sugar molecule (deoxyribose), a phosphate group, and a nitrogenous base. There are four types of nitrogenous bases in DNA: adenine (A), guanine (G), cytosine (C), and thymine (T). Adenine pairs with thymine, and guanine pairs with cytosine, forming the rungs of the ladder that make up the double helix.

The genetic information in DNA is encoded in the sequence of these nitrogenous bases. Large sequences of bases form genes, which provide the instructions for the production of proteins. The process of gene expression involves transcribing the DNA sequence into a complementary RNA molecule, which is then translated into a protein.

Plant DNA is similar to animal DNA in many ways, but there are also some differences. For example, plant DNA contains a higher proportion of repetitive sequences and transposable elements, which are mobile genetic elements that can move around the genome and cause mutations. Additionally, plant cells have cell walls and chloroplasts, which are not present in animal cells, and these structures contain their own DNA.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Membrane transport proteins are specialized biological molecules, specifically integral membrane proteins, that facilitate the movement of various substances across the lipid bilayer of cell membranes. They are responsible for the selective and regulated transport of ions, sugars, amino acids, nucleotides, and other molecules into and out of cells, as well as within different cellular compartments. These proteins can be categorized into two main types: channels and carriers (or pumps). Channels provide a passive transport mechanism, allowing ions or small molecules to move down their electrochemical gradient, while carriers actively transport substances against their concentration gradient, requiring energy usually in the form of ATP. Membrane transport proteins play a crucial role in maintaining cell homeostasis, signaling processes, and many other physiological functions.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Proteomics is the large-scale study and analysis of proteins, including their structures, functions, interactions, modifications, and abundance, in a given cell, tissue, or organism. It involves the identification and quantification of all expressed proteins in a biological sample, as well as the characterization of post-translational modifications, protein-protein interactions, and functional pathways. Proteomics can provide valuable insights into various biological processes, diseases, and drug responses, and has applications in basic research, biomedicine, and clinical diagnostics. The field combines various techniques from molecular biology, chemistry, physics, and bioinformatics to study proteins at a systems level.

Eukaryota is a domain that consists of organisms whose cells have a true nucleus and complex organelles. This domain includes animals, plants, fungi, and protists. The term "eukaryote" comes from the Greek words "eu," meaning true or good, and "karyon," meaning nut or kernel. In eukaryotic cells, the genetic material is housed within a membrane-bound nucleus, and the DNA is organized into chromosomes. This is in contrast to prokaryotic cells, which do not have a true nucleus and have their genetic material dispersed throughout the cytoplasm.

Eukaryotic cells are generally larger and more complex than prokaryotic cells. They have many different organelles, including mitochondria, chloroplasts, endoplasmic reticulum, and Golgi apparatus, that perform specific functions to support the cell's metabolism and survival. Eukaryotic cells also have a cytoskeleton made up of microtubules, actin filaments, and intermediate filaments, which provide structure and shape to the cell and allow for movement of organelles and other cellular components.

Eukaryotes are diverse and can be found in many different environments, ranging from single-celled organisms that live in water or soil to multicellular organisms that live on land or in aquatic habitats. Some eukaryotes are unicellular, meaning they consist of a single cell, while others are multicellular, meaning they consist of many cells that work together to form tissues and organs.

In summary, Eukaryota is a domain of organisms whose cells have a true nucleus and complex organelles. This domain includes animals, plants, fungi, and protists, and the eukaryotic cells are generally larger and more complex than prokaryotic cells.

Proton-translocating ATPases are complex, multi-subunit enzymes found in the membranes of many organisms, from bacteria to humans. They play a crucial role in energy transduction processes within cells.

In simpler terms, these enzymes help convert chemical energy into a form that can be used to perform mechanical work, such as moving molecules across membranes against their concentration gradients. This is achieved through a process called chemiosmosis, where the movement of ions (in this case, protons or hydrogen ions) down their electrochemical gradient drives the synthesis of ATP, an essential energy currency for cellular functions.

Proton-translocating ATPases consist of two main domains: a catalytic domain responsible for ATP binding and hydrolysis, and a membrane domain that contains the ion transport channel. The enzyme operates in either direction depending on the energy status of the cell: it can use ATP to pump protons out of the cell when there's an excess of chemical energy or utilize the proton gradient to generate ATP during times of energy deficit.

These enzymes are essential for various biological processes, including nutrient uptake, pH regulation, and maintaining ion homeostasis across membranes. In humans, they are primarily located in the inner mitochondrial membrane (forming the F0F1-ATP synthase) and plasma membranes of certain cells (as V-type ATPases). Dysfunction of these enzymes has been linked to several diseases, including neurological disorders and cancer.

Cytochrome f is a type of cytochrome protein that contains heme as a cofactor and plays a role in the electron transport chain during photosynthesis. It is specifically located in the cytochrome b6f complex, which is found in the thylakoid membrane of chloroplasts in plants and algae.

Cytochrome f functions as a ubiquinol-plastoquinone oxidoreductase, accepting electrons from ubiquinol and transferring them to plastoquinone. This electron transfer process is an essential step in the generation of a proton gradient across the thylakoid membrane, which drives the synthesis of ATP during photosynthesis.

Deficiency or mutation in cytochrome f can lead to impaired photosynthetic efficiency and reduced growth in plants.

'Toxic plants' refer to those species of plants that contain toxic substances capable of causing harmful effects or adverse health reactions in humans and animals when ingested, touched, or inhaled. These toxins can cause a range of symptoms from mild irritation to serious conditions such as organ failure, paralysis, or even death depending on the plant, the amount consumed, and the individual's sensitivity to the toxin.

Toxic plants may contain various types of toxins, including alkaloids, glycosides, proteins, resinous substances, and essential oils. Some common examples of toxic plants include poison ivy, poison oak, nightshade, hemlock, oleander, castor bean, and foxglove. It is important to note that some parts of a plant may be toxic while others are not, and the toxicity can also vary depending on the stage of growth or environmental conditions.

If you suspect exposure to a toxic plant, it is essential to seek medical attention immediately and, if possible, bring a sample of the plant for identification.

A plant genome refers to the complete set of genetic material or DNA present in the cells of a plant. It contains all the hereditary information necessary for the development and functioning of the plant, including its structural and functional characteristics. The plant genome includes both coding regions that contain instructions for producing proteins and non-coding regions that have various regulatory functions.

The plant genome is composed of several types of DNA molecules, including chromosomes, which are located in the nucleus of the cell. Each chromosome contains one or more genes, which are segments of DNA that code for specific proteins or RNA molecules. Plants typically have multiple sets of chromosomes, with each set containing a complete copy of the genome.

The study of plant genomes is an active area of research in modern biology, with important applications in areas such as crop improvement, evolutionary biology, and medical research. Advances in DNA sequencing technologies have made it possible to determine the complete sequences of many plant genomes, providing valuable insights into their structure, function, and evolution.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Mesophyll cells are photosynthetic cells located in the interior tissue of a leaf, specifically within the chloroplast-containing portion called the mesophyll. These cells are responsible for capturing sunlight and converting it into chemical energy through the process of photosynthesis. They can be further divided into two types: palisade mesophyll cells and spongy mesophyll cells.

Palisade mesophyll cells are columnar-shaped cells that contain many chloroplasts and are located closer to the upper epidermis of the leaf. They are arranged in one or more layers and are primarily responsible for capturing light during photosynthesis.

Spongy mesophyll cells, on the other hand, are loosely arranged and have a sponge-like structure. They contain fewer chloroplasts than palisade mesophyll cells and are located closer to the lower epidermis of the leaf. These cells facilitate gas exchange between the plant and the environment by allowing for the diffusion of carbon dioxide into the leaf and oxygen out of the leaf.

Overall, mesophyll cells play a critical role in photosynthesis and help to maintain the health and growth of the plant.

Diuron is a pesticide and herbicide that is used to control weeds in various settings, such as agriculture, landscaping, and forestry. Its chemical name is 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Diuron works by inhibiting photosynthesis in plants, which prevents them from growing and eventually kills them.

While diuron is effective at controlling weeds, it can also have harmful effects on non-target organisms, including aquatic life and pollinators. Additionally, there are concerns about the potential for diuron to contaminate water sources and pose risks to human health. As a result, its use is regulated in many countries, and there are restrictions on how it can be applied and disposed of.

It's worth noting that Diuron is not a medical term or a drug used for treating any medical condition in humans or animals.

Edible plants are those that can be safely consumed by humans and other animals as a source of nutrition. They have various parts (such as fruits, vegetables, seeds, roots, stems, and leaves) that can be used for food after being harvested and prepared properly. Some edible plants have been cultivated and domesticated for agricultural purposes, while others are gathered from the wild. It is important to note that not all plants are safe to eat, and some may even be toxic or deadly if consumed. Proper identification and knowledge of preparation methods are crucial before consuming any plant material.

'Acetabularia' is a genus of large, single-celled marine algae that are commonly found in warm and temperate coastal waters. These algae are characterized by their distinctive umbrella-shaped cap, known as the "acetabulum," which sits atop a long, slender stalk. The acetabulum contains reproductive structures, while the stalk contains the nucleus of the cell. 'Acetabularia' species are notable for their ability to survive and grow even when their nuclei are removed, making them a subject of interest in studies of cell biology and regeneration.

I'm sorry for any confusion, but "Hordeum" is not a medical term. It is actually the genus name for barley in botany. If you have any medical terms or concepts that you would like me to explain, please let me know!

RNA editing is a process that alters the sequence of a transcribed RNA molecule after it has been synthesized from DNA, but before it is translated into protein. This can result in changes to the amino acid sequence of the resulting protein or to the regulation of gene expression. The most common type of RNA editing in mammals is the hydrolytic deamination of adenosine (A) to inosine (I), catalyzed by a family of enzymes called adenosine deaminases acting on RNA (ADARs). Inosine is recognized as guanosine (G) by the translation machinery, leading to A-to-G changes in the RNA sequence. Other types of RNA editing include cytidine (C) to uridine (U) deamination and insertion/deletion of nucleotides. RNA editing is a crucial mechanism for generating diversity in gene expression and has been implicated in various biological processes, including development, differentiation, and disease.

Plastoquinone is a lipid-soluble electron carrier in the photosynthetic electron transport chain located in the thylakoid membrane of chloroplasts. It plays a crucial role in both the light-dependent reactions of photosynthesis and cyclic photophosphorylation.

In more detail, plastoquinone exists in an oxidized (PQ) and reduced form (PQH2). In its oxidized state, it accepts electrons from cytochrome b6f complex during the transfer of electrons from photosystem II to photosystem I. Once plastoquinone accepts two electrons and two protons, it converts into its reduced form, plastoquinol (PQH2). Plastoquinol then donates the electrons to the cytochrome b6f complex, which in turn passes them on to the next carrier in the electron transport chain.

Plastoquinone is a member of the quinone family and is synthesized via the methylerythritol 4-phosphate (MEP) pathway, also known as the non-mevalonate pathway.

Angiosperms, also known as flowering plants, are a group of plants that produce seeds enclosed within an ovary. The term "angiosperm" comes from the Greek words "angeion," meaning "case" or "capsule," and "sperma," meaning "seed." This group includes the majority of plant species, with over 300,000 known species.

Angiosperms are characterized by their reproductive structures, which consist of flowers. The flower contains male and female reproductive organs, including stamens (which produce pollen) and carpels (which contain the ovules). After fertilization, the ovule develops into a seed, while the ovary matures into a fruit, which provides protection and nutrition for the developing embryo.

Angiosperms are further divided into two main groups: monocots and eudicots. Monocots have one cotyledon or embryonic leaf, while eudicots have two. Examples of monocots include grasses, lilies, and orchids, while examples of eudicots include roses, sunflowers, and legumes.

Angiosperms are ecologically and economically important, providing food, shelter, and other resources for many organisms, including humans. They have evolved a wide range of adaptations to different environments, from the desert to the ocean floor, making them one of the most diverse and successful groups of plants on Earth.

I'm happy to help! However, I believe there might be a slight confusion in your question. RNA stands for "ribonucleic acid," which is a type of nucleic acid that plays a crucial role in biology, particularly in the process of gene expression. It's important to note that "algal" generally refers to something related to algae, which are simple, photosynthetic organisms.

There isn't a specific medical definition for "Algal RNA." However, if you're referring to RNA found in algae or RNA with a role in algal biology, then the definition would be as follows:

RNA is a nucleic acid present in algae that carries genetic information and is involved in various cellular processes. Algal RNA can exist in several forms, including messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA). These RNAs play essential roles in protein synthesis, regulation of gene expression, and other cellular functions within algae.

If you meant something different by "Algal RNA," please provide more context or clarify your question, and I'll be glad to help further!

Fructose-bisphosphatase (FBPase) is an enzyme that plays a crucial role in the regulation of gluconeogenesis, which is the process of generating new glucose molecules from non-carbohydrate sources in the body. Specifically, FBPase is involved in the fourth step of gluconeogenesis, where it catalyzes the conversion of fructose-1,6-bisphosphate to fructose-6-phosphate.

Fructose-1,6-bisphosphate is a key intermediate in both glycolysis and gluconeogenesis, and its conversion to fructose-6-phosphate represents an important regulatory point in these pathways. FBPase is inhibited by high levels of energy charge (i.e., when the cell has plenty of ATP and low levels of ADP), as well as by certain metabolites such as citrate, which signals that there is abundant energy available from other sources.

There are two main isoforms of FBPase in humans: a cytoplasmic form found primarily in the liver and kidney, and a mitochondrial form found in various tissues including muscle and brain. Mutations in the gene that encodes the cytoplasmic form of FBPase can lead to a rare inherited metabolic disorder known as fructose-1,6-bisphosphatase deficiency, which is characterized by impaired gluconeogenesis and hypoglycemia.

Plastocyanin is a small, copper-containing protein that plays a crucial role in the photosynthetic electron transport chain. It functions as an electron carrier, facilitating the movement of electrons between two key protein complexes (cytochrome b6f and photosystem I) located in the thylakoid membrane of chloroplasts. Plastocyanin is a soluble protein found in the lumen of the thylakoids, and its copper ion serves as the site for electron transfer. The oxidized form of plastocyanin accepts an electron from cytochrome b6f and then donates it to photosystem I, helping to maintain the flow of electrons during light-dependent reactions in photosynthesis.

Group I chaperonins are a family of protein complexes that assist in the folding and assembly of other proteins. They are found in archaea and the eukaryotic cytosol, and are characterized by their barrel-shaped structure with a central cavity where unfolded proteins bind and are folded with the help of ATP hydrolysis. In humans, Group I chaperonins include the HSP60 (heat shock protein 60) and CCT (cytosolic chaperonin containing TCP-1) complexes. These chaperonins play crucial roles in various cellular processes such as protein quality control, protein trafficking, and signal transduction.

... chloroplast protein-importing). Cline K, Ettinger WF, Theg SM (1992). "Protein-specific energy requirements for protein ... "Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport". ... In enzymology, a chloroplast protein-transporting ATPase (EC is an enzyme that catalyzes the chemical reaction ATP + ... Scott SV, Theg SM (1996). "A new chloroplast protein import intermediate reveals distinct translocation machineries in the two ...
These proteins also help the polypeptide get imported into the chloroplast. From here, chloroplast proteins bound for the ... the new chloroplast host had to develop a unique protein targeting system to avoid having chloroplast proteins being sent to ... Protein synthesis within chloroplasts relies on two RNA polymerases. One is coded by the chloroplast DNA, the other is of ... Though chloroplast DNA is not associated with true histones, in red algae, similar proteins that tightly pack each chloroplast ...
... a histone-like chloroplast protein (HC) coded by the chloroplast DNA that tightly packs each chloroplast DNA ring into a ... the new chloroplast host had to develop a unique protein targeting system to avoid having chloroplast proteins being sent to ... A protein kinase drifting around on the outer chloroplast membrane can use ATP to add a phosphate group to the Toc34 protein, ... As a result, protein synthesis must be coordinated between the chloroplast and the nucleus. The chloroplast is mostly under ...
Chloroplasts genomes encode 50-200 proteins, compared to the thousands in cyanobacterium. Furthermore, in Arabidopsis, nearly ... Chloroplasts contain 16S rRNA and 23S rRNA. 16S and 23S rRNA is found only in prokaryotes by definition. Chloroplasts and ... Harris EH, Boynton JE, Gillham NW (December 1994). "Chloroplast ribosomes and protein synthesis". Microbiological Reviews. 58 ( ... Pollen was thought not to be able to transfer chloroplast DNA in tobacco (which later turned out not to be as true as was ...
Algal and plant chloroplast S16. * Cyanelle S16. * Neurospora crassa mitochondrial S24 (cyt-21). S16 proteins have about 100 ... Ribosomal protein S16 is one of the proteins from the small ribosomal subunit. It belongs to a ribosomal protein family that is ... The protein belongs to the S9P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ... 40S ribosomal protein S16' is a protein that in humans is encoded by the RPS16 gene. Ribosomes, the organelles that catalyze ...
Permeability of chloroplast envelopes to Mg2+. Effects on protein synthesis. Plant Physiol. 74, 956-961 Stirling, C.J., ... to tether cellular proteins to a ubiquitin ligase, resulting in ubiquitination and degradation of the tethered protein. This ... Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. ... Protein translocation: As a graduate student and postdoctoral fellow working with Dr. Randy Schekman at the University of ...
Jarvis P, Soll J (December 2001). "Toc, Tic, and chloroplast protein import". Biochimica et Biophysica Acta (BBA) - Molecular ... Channel proteins called porins in the outer membrane allow free diffusion of ions and small proteins about 5000 daltons or less ... mainly assist the translocation of chloroplast precursor proteins Chaperone involvement in the IMS has been proposed but still ... The IMS is involved in the mitochondrial protein translocation. The precursor proteins called small TIM chaperones which are ...
Instead, chloroplast genes encoded in chloroplast DNA are found on numerous 2-3 kbp minicircles, analogous to plasmids. Most ... minicircles have only a few protein-coding genes; many have just a single gene. There are reports of minicircles that do not ... have chloroplasts. The Amphidinium chloroplast genome is unusual in not having a single contiguous circular genome. ... Clade C3 chloroplast genome. Minicircle-derived transcripts can be processed in ways not typical of eukaryotes, including the ...
"Motif analysis unveils the possible co-regulation of chloroplast genes and nuclear genes encoding chloroplast proteins". Plant ... Pfalz J, Pfannschmidt T (April 2013). "Essential nucleoid proteins in early chloroplast development". Trends in Plant Science. ... Eukaryotic chloroplasts, as well as the other plant plastids, also contain extrachromosomal DNA molecules. Most chloroplasts ... For example, cpDNA content in the chloroplasts of young cells, during the early stages of development where the chloroplasts ...
Proteins may be targeted to several sites of the chloroplast depending on their sequences such as the outer envelope, inner ... Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate ... Within the ER, the protein is first covered by a chaperone protein to protect it from the high concentration of other proteins ... Many proteins are needed in both mitochondria and chloroplasts. In general the dual-targeting peptide is of intermediate ...
"Protein synthesis in chloroplasts. I. Light-driven synthesis of the large subunit of Fraction I protein by isolated pea ... Barraclough, R.; Ellis, R. J. (1980). "Protein synthesis in chloroplasts IX. Assembly of newly-synthesised large subunits into ... 1973: First identification of a product of protein synthesis by chloroplast ribosomes. 1978: First demonstration of in vitro ... "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330-334. Bibcode:1988Natur. ...
... the protein product of which stabilised the pigment-protein-lipid complexes of chloroplasts so that dying leaves remained green ... Chloroplast proteins and chlorophyll catabolites during foliar senescence. New Phytologist 126 593-600 P Matile, S Ginsburg, M ... chloroplast proteins and chlorophyll catabolites during foliar senescence". New Phytologist. 126 (4): 593-600. doi:10.1111/j. ... This work made a substantial contribution to the understanding of the catabolism of chloroplasts and chlorophylls. He began to ...
... protein located in plant chloroplasts. Using selective inhibitors of protein synthesis Cashmore showed that in contrast to the ... The soluble precursor protein is subsequently processed and imported into chloroplasts. At Rockefeller University, Cashmore ... Cashmore, AR (1976). "Protein Synthesis in Plant Leaf Tissue: The sites of synthesis of the major proteins" (PDF). Journal of ... Lubben, TH; Theg, SM; Keegstra, K (1988). "Transport of proteins into chloroplasts". Photosynthesis Research. 17 (1-2): 173-194 ...
In the chloroplasts of the unicellular algae Chlamydomonas reinhardtii the protein disulfide-isomerase RB60 serves as a redox ... Protein disulfide-isomerase has been found to be involved in the breaking of bonds on the HIV gp120 protein during HIV ... More specifically, protein disulfide-isomerase can no longer fix misfolded proteins once its thiol group in its active site has ... Perri ER, Thomas CJ, Parakh S, Spencer DM, Atkin JD (2016). "The Unfolded Protein Response and the Role of Protein Disulfide ...
Leckband worked with Martin Gruebele to understand the stability of proteins in situ at sub-micron resolution. Their research ... Leckband, Deborah Elaine (1988). "A kinetic study of nucleotide interactions with chloroplast coupling factor". Leckband, ... D Leckband (January 1, 2000). "Measuring the forces that control protein interactions". Annual Review of Biophysics and ... Leckband, Deborah (August 1995). "The surface force apparatus - a tool for probing molecular protein interactions". Nature. 376 ...
Deshaies, R. J.; Fish, L. E.; Jagendorf, A. T. (1984). "Permeability of Chloroplast Envelopes to Mg2+: Effects on Protein ... The metabolic state of the chloroplast changes considerably between night and day. During the day, the chloroplast is actively ... "Effect of divalent cations on cation fluxes across the chloroplast envelope and on photosynthesis of intact chloroplasts". ... To date, only the ZntA protein of Paramecium has been shown to be a Mg2+ channel. The mechanisms of Mg2+ transport by the ...
Boudreau E, Takahashi Y, Lemieux C, Turmel M, Rochaix JD (October 1997). "The chloroplast ycf3 and ycf4 open reading frames of ... Protein pages needing a picture, Protein families, Protein domains, Photosynthesis, All stub articles, Plant physiology stubs, ... In molecular biology, the Ycf4 protein is involved in the assembly of the photosystem I complex which is part of an energy- ... The Ycf4 protein is firmly associated with the thylakoid membrane, presumably through a transmembrane domain. Ycf4 co- ...
A similar protein structure exists in the chloroplast of certain plants. This protein presence provides evidence for the ... Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1 Heat shock protein 60 (HSP60) is a mitochondrial chaperonin that ... The role of the phage encoded gp31 protein appears be to interact with the E. coli host encoded GroEL protein to assist in the ... Heat shock proteins are primarily responsible for maintaining the integrity of cellular proteins particularly in response to ...
A homolog (B5X582) is found in Arabidopsis thaliana chloroplast and mitochondria. In 2001, a team was able to identify the ... Twinkle protein also known as twinkle mtDNA helicase is a mitochondrial protein that in humans is encoded by the TWNK gene ( ... The gene encodes for a protein that has a full-length of 684 units of amino acids. The twinkle protein consists of 3 functional ... The TWNK gene makes two proteins, Twinkle and Twinky. The proteins Twinkle and Twinky are both found in the mitochondria. Each ...
DeBlasio SL, Luesse DL, Hangarter RP (September 2005). "A plant-specific protein essential for blue-light-induced chloroplast ... Integral membrane proteins, Molecular biology, Plant physiology, EC 2.7.11, All stub articles, Membrane protein stubs). ... Phototropins may also be important for the opening of stomata and the movement of chloroplasts. These blue light receptors are ... Phototropins have been shown to impact the movement of chloroplast inside the cell. In addition phototropins mediate the first ...
"Functional analysis of the Chloroplast GrpE (CGE) proteins from Arabidopsis thaliana". Plant Physiology and Biochemistry. 139: ... Once DnaJ, a co-chaperone, brings an unfolded protein to DnaK ATP is hydrolyzed to ADP to facilitate folding of the protein. At ... GrpE (Gro-P like protein E) is a bacterial nucleotide exchange factor that is important for regulation of protein folding ... The thermal regulation of DnaK slows protein folding and prevents unfolded proteins from accumulating in the cytoplasm at high ...
The Chloroplast Envelope Anion Channel-forming Tic110 (Tic110) Family (TC#1.A.18) consists of proteins of the inner chloroplast ... Protein families, Membrane proteins, Transmembrane proteins, Transmembrane transporters, Transport proteins, Integral membrane ... van den Wijngaard, P. W.; Vredenberg, W. J. (1999-09-03). "The envelope anion channel involved in chloroplast protein import is ... Kessler, F.; Blobel, G. (1996-07-23). "Interaction of the protein import and folding machineries of the chloroplast". ...
The site of replication is unknown but it is thought to be in the chloroplast and in the presence of Mg2+ ions. Predictions of ... Key features of replication include no helper virus required and no proteins are encoded for. Unlike the other family of ... Replication occurs in the chloroplasts of plant cells. ...
Some other proteins are inserted into the membrane via the SRP (signal recognition particle) pathway. The chloroplast SRP can ... which binds to the imported protein and a Sec membrane complex to shuttle the protein across. Proteins with a twin arginine ... Chloroplasts have their own genome, which encodes a number of thylakoid proteins. However, during the course of plastid ... After entering the chloroplast, the first targeting peptide is cleaved off by a protease processing imported proteins. This ...
Stearl-acyl Carrier Protein Desaturase from Spinach Chloroplasts". Plant Physiology. 54 (4): 484-486. doi:10.1104/pp.54.4.484. ... Schultz, D; Suh, M.; Ohlrogge (2000). "Stearoyl-Acyl Carrier Protein and Unusual Acyl-Acyl Carrier Protein Desaturase ... acyl-carrier-protein] + acceptor + 2 H2O The systematic name of this enzyme class is acyl-[acyl-carrier-protein], hydrogen- ... "Stearoyl-acyl carrier protein delta 9 desaturase from Ricinus communis is a diiron-oxo protein". Proceedings of the National ...
When translating from genome to protein, the use of the correct genetic code is essential. The mitochondrial codes are the ... all plant chloroplast differences due to RNA edit. Table 15 is deleted in the source but included here for completeness. Other ... mechanisms also play a part in protein biosynthesis, such as post-transcriptional modification. Watanabe, Kimitsuna; Suzuki, ...
August 2004). "Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors". Plant ... magnesium or zinc deficient nitrogen and/or proteins a soil pH at which minerals become unavailable for absorption by the roots ...
Zhang, Xinchun; Hu, Jianping (February 2010). "The Arabidopsis Chloroplast Division Protein DYNAMIN-RELATED PROTEIN5B Also ... A third research area encompasses structural and functional studies of proteins that are used to construct subcellular ... Aung, Kyaw; Hu, Jianping (2011-12-01). "The Arabidopsis Tail-Anchored Protein PEROXISOMAL AND MITOCHONDRIAL DIVISION FACTOR1 Is ... March 22, 2019). "Structural Characterization of a Synthetic Tandem-Domain Bacterial Microcompartment Shell Protein Capable of ...
... "β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts". The Plant Journal. 79 (1): 1-12. ... "A Zinc Finger Motif-Containing Protein Is Essential for Chloroplast RNA Editing". PLOS Genetics. 11 (3): e1005028. doi:10.1371/ ... a member of an Arabidopsis protein family, interacts with the protein RARE1 and broadly affects RNA editing". Proceedings of ... Most of the Rf genes cloned from other species have been found to be PPR proteins. Hanson's group was the first to utilize GFP ...
They also recorded increased levels of DNA repair-associated proteins and reactive oxygen species (ROS)-detox. ROS is a product ... They recorded increased nucleotide substitution rates in chloroplast, mitochondrial, and cellular genomes. ...
... chloroplast protein-importing). Cline K, Ettinger WF, Theg SM (1992). "Protein-specific energy requirements for protein ... "Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport". ... In enzymology, a chloroplast protein-transporting ATPase (EC is an enzyme that catalyzes the chemical reaction ATP + ... Scott SV, Theg SM (1996). "A new chloroplast protein import intermediate reveals distinct translocation machineries in the two ...
maturase K (chloroplast) [Vaccinium consanguineum] maturase K (chloroplast) [Vaccinium consanguineum]. gi,18029400,gb, ... The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in ... The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in ...
Chloroplasts, Genes, Reporter, Luminescent Proteins, Promoter Regions, Genetic, Protein Engineering, Recombinant Proteins. ... Improving recombinant protein production in the Chlamydomonas reinhardtii chloroplast using vivid Verde Fluorescent Protein as ... Improving recombinant protein production in the Chlamydomonas reinhardtii chloroplast using vivid Verde Fluorescent Protein as ... Improving recombinant protein production in the Chlamydomonas reinhardtii chloroplast using vivid Verde Fluorescent Protein as ...
2009) Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network. FEBS ... Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network ... Little is known about the mobility of proteins within this system. We studied a stromal lamellae protein, Hcf106, by targeting ... The protein is thus either immobile within the thylakoid membrane, or its diffusion is tightly restricted within distinct ...
The role of plastid heat shock proteins during singlet oxygen induced chloroplast stress. Marta Kozlowska, Graduate Student, ... The role of plastid heat shock proteins during singlet oxygen induced chloroplast stress. *Home ... The role of plastid heat shock proteins during singlet oxygen induced chloroplast stress ... Small heat shock proteins (sHSPs) have been shown to play a role in the molecular response to 1O2. Using a genetics approach, ...
Light-driven synthesis of the large subunit of fraction I protein by isolated chloroplasts. scientific article published on ... Light-driven synthesis of the large subunit of fraction I protein by isolated chloroplasts (English) ... Photosynthetic phosphorylation as energy source for protein synthesis and carbon dioxide assimilation by chloroplasts ... Non-synchronous incorporation of C14O2 into amino acids of the two subunits of fraction I protein ...
... emphasizing chloroplast-related proteins. We have highlighted current advances regarding chloroplast-related proteins role in ... Chloroplasts and Chloroplast-Related Proteins Facilitate the Viral Replication Cycle of Plant (+)ss RNA Viruses. The viral ... However, more chloroplast-related proteins must be determined to understand the proteins involved in host defense accurately. ... Characterization of proteins involved in chloroplast targeting disturbed by rice stripe virus by novel protoplast-chloroplast ...
Paspalum distichum bio-material USDA:GRIN:PI222796 ribosomal protein L16 (rpl16) gene, intron; chloroplast ... Paspalum distichum bio-material USDA:GRIN:PI364977 ribosomal protein L16 (rpl16) gene, intron; chloroplast ... Paspalum distichum bio-material USDA:GRIN:PI647916 ribosomal protein L16 (rpl16) gene, intron; chloroplast ... indutum voucher YDK2009778 PsbA (psbA) gene, partial cds; psbA-trnH intergenic spacer, complete sequence; ribosomal protein S19 ...
... which from now on aims to become a global repository for all transmembrane β-barrel proteins, both eukaryotic and bacterial. ... which from now on aims to become a global repository for all transmembrane β-barrel proteins, both eukaryotic and bacterial. ... was introduced as a database for β-barrel outer membrane proteins from Gram-negative bacteria in 2011 and then included 69,354 ... was introduced as a database for β-barrel outer membrane proteins from Gram-negative bacteria in 2011and then included 69,354 ...
... had chloroplasts that carried genes coding for a resistance to another antibiotic and a green fluorescent protein. After the ... The new chloroplast genome can even be handed down to the next generation and, thereby, give a plant new traits. These findings ... Researchers Discover Chloroplast Genomes Transfer from Plant to Plant. TOPICS:DNAGene TransferGenomeMax Planck Institute ... "The new chloroplasts had kept their entire genetic information and fully ousted the old ones. They were even inherited by the ...
2014); both quickly-evolving proteins and also proteins in which there appeared to be much parallel evolution in Cryptomeria ... 2003: large chloroplast data set; Quandt et al. 2004: trnL intron; C.-S. Wu et al. 2012b: LBA, 2013: some analyses). If this ... 2012) discuss the evolution of transcription-associated proteins, perhaps linked with genome duplications; three new protein ... 2014, both whole chloroplast genomes; Davis et al. 2014a; Magallón et al. 2015; He et al. 2015; Sen et al. 2016; S.-M. Chaw et ...
maintenance of protein localization in endoplasmic reticulum +. 16. maintenance of protein location in chloroplast. 0. ... maintenance of protein localisation to organelle; maintenance of protein localization to organelle. ... Protein-Protein Interactions) PhenoMiner (Quatitative Phenotypes) Gene Annotator OLGA (Gene List Generator) AllianceMine ... G protein-coupled receptor kinase 2. IMP. RGD. PMID:28759639. RGD:13513977. NCBI chr 1:201,580,823...201,601,580 Ensembl chr 1: ...
The import of chloroplast proteins synthesized in the cytosol of a plant cell is mediated by two multiprotein complexes or ... The plant PRAT proteins - preprotein and amino acid transport in mitochondria and chloroplasts. ... These complexes integrate different signals to assure the timely transport of proteins into the chloroplast in accordance with ... Redox-regulation of protein import into chloroplasts and mitochondria: Similarities and differences.. ...
1998 - 1999 Expression of nuclear genes for chloroplast ribosomal proteins.. *1997 - 1999 Molecular breeding studies on crop ... 1996 - 1997 Nuclear encoded chloroplast ribosomal protein genes ; genomic structure and organ-specific gene expression. ...
PSB33 protein sustains Photosystem II in plant chloroplasts under UVA light. Anders K. Nilsson, Aleš Pěnčík, Oskar N. Johansson ... PSB33 sustains photosystem II D1 protein under fluctuating light conditions R. Fristedt, A. Trotta, M. Suorsa, Anders K. ... The development of blood protein profiles in extremely preterm infants follows a stereotypic evolution pattern ...
The identification of the proteins oxidatively modified in Met residues revealed the finding that MetO-containing proteins are ... CNBr treatment of proteins causes the non-enzymatic hydrolysis of peptide bonds on the carboxyl side of reduced Met residues. ... Then, the 2Dd-CNBr method was applied to the Arabidopsis thaliana seed protein extract in a control (non-oxidized) condition ... This approach was first validated using bovine serum albumin as a model protein, which confirmed the possibility of ...
Regulation of chloroplast translation: interactions of RNA elements, RNA-binding proteins and the plastid ribosome ... Open the PDF for ,span class=search-highlight,Chloroplast,/span, RNA-binding and pentatricopeptide repeat proteins in another ... A. Di Cola; E. Klostermann; C. Robinson Numerous proteins are transported into or across the chloroplast thylakoid membrane. To ... In the present study, we focus on two RNA-binding proteins: cpRNP (chloroplast ribonucleoprotein) and PPR... ...
Reactivity and protein-protein interaction of human peroxidasin 1. Autoren: Furtmüller, P.G, Paumann-Page, M; Pfanzagl, V; ... Hydroperoxidases in oxygenic phototrophic prokaryotes- comparison to plant chloroplasts. Autoren: Regelsberger, G., Jakopitsch ... Heme to protein linkages in mammalian peroxidases. Autoren: Stampler, J., Zederbauer, M., Furtmüller, P.G., Obinger, C. ... 2005) Protein-based radical intermediates in bifunctional heme peroxidases. Autoren: Ivancich, A., Un, S., Obinger, C., Loewen ...
The energetics of the chloroplast Tat system (Alder and Theg, 2003; Berks et al., 2005; Theg et al., 2005) suggest a protein:H+ ... Folded protein or protein domain (cytoplasm) + energy → Folded protein or protein domain (out) (periplasm of Gram-negative ... Although the Rieske protein in most organisms is a monotopic membrane protein, in actinobacteria, it is a polytopic protein ... 2000). TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in Sec-independent protein ...
We have established iCLIP for plants to identify target transcripts of the RNA-binding protein AtGRP7. This paves the way to ... wide to determine the binding repertoire of the circadian clock-regulated Arabidopsis thaliana glycine-rich RNA-binding protein ... vivo binding targets and binding landscapes represents a gap in understanding the mode of action of plant RNA-binding proteins ... Functions for RNA-binding proteins in orchestrating plant development and environmental responses are well established. However ...
Protein sorting. Process of targeting proteins to specific compartments (i.e. mitochondria, chloroplasts, peroxisomes, RER). ... transmembrane proteins become integral proteins of plasma membrane - i.e. receptors or transport proteins); proteins in lumen ... Protein orientation. As passage of protein through intracellular membrane continues, if amino end of protein faces lumen of ER ... Targeting protein to specific compartment; newly translated region on protein that is bound by docking protein, which in turn ...
Plant FAX Proteins - The Flow of Fatty Acids from Chloroplasts to ER (and Beyond?) ... Structural Analysis and Aggregation of Proteins in Solution and Poration of Endosomal Membranes by a Comparative Study using ... The Dynamic Mitochondrion and Chloroplasts Discussion Leader: Shey-Shing Sheu (Thomas Jefferson University, United States) ... Sterol Homeostasis in Vacuoles of Saccharomyces Cerevisiae Mediated by Niemann-Pick Type C Related Protein 1 ...
N2 - Reactive oxygen species (ROS)-dependent signaling pathways from chloroplasts and mitochondria merge at the nuclear protein ... AB - Reactive oxygen species (ROS)-dependent signaling pathways from chloroplasts and mitochondria merge at the nuclear protein ... Reactive oxygen species (ROS)-dependent signaling pathways from chloroplasts and mitochondria merge at the nuclear protein ... dependent signaling pathways from chloroplasts and mitochondria merge at the nuclear protein RADICAL-INDUCED CELL DEATH1 (RCD1 ...
A Z protein associated with PS II splits water into oxygen, protons, electrons • Oxygen leaves chloroplast as a by-product • 2 ... Chloroplasts • Typical plant cell chloroplast approx. 3um to 8um in length and 2 um to 3 um in diameter • Have two limiting ... Occurs in plant chloroplasts, producing g________ and ATP. Photosynthesis. Occurs in plant chloroplasts, producing g________ ... The chloroplasts of plants use a process called photosynthesis to capture light energy from the sun and convert it to chemical ...
"DIVERSITY IN PHOSPHORYLATION OF THYLAKOID MEMBRANE PROTEINS IN CHLOROPLASTS" at the University of Turku on 09 April 2024 at ... My thesis explores the regulation of photosynthesis through protein phosphorylations, mainly by thylakoid-associated protein ... Additionally, I discovered that calcium signaling, along with thylakoid protein phosphorylations, modulates the key proteins ... Notably, I found that the formation of a moss-specific PSI Large protein complex relies on the phosphorylation of specific ...
Preparation of Chloroplast Sub-compartments from Arabidopsis for the Analysis of Protein Localization by Immunoblotting or ... Immunization of Alpacas (Lama pacos) with Protein Antigens and Production of Antigen-specific Single Domain Antibodies ...
... chloroplast development, and photosynthesis system. In this study, the yellow leaf 1 (yl1) rice mutant was identified from the ... Most proteins localized in chloroplasts are the coding products of nuclear genes. Thus, the mutation of genes involved in the ... 2.6 Protein Subcellular Localization. To determine the subcellular localization of the LOC_Os03g36760 protein, the pCambia-35S ... Abnormal chloroplast development causes changes in the normal proportion and content of each chloroplast pigment, which is ...
Native architecture of the Chlamydomonas chloroplast revealed by in situ cryo-electron tomography. Elife 4, 1-29. p.10 2nd ... Percent of protein in crop leaves that is RuBisCO (most abundant protein). ... Fraction of soluble protein in rice and wheat leaves that is comprised of RuBisCO. ... The isolation and partial characterization of the pyrenoid protein of Eremosphaera viridis. The Journal of Cell Biology 51 :499 ...
The PyDET2e protein was localized in chloroplasts; (4) Conclusions: The PyDET2e is involved in the development of P. ... Using Arabidopsis protein prenyltransferase loss-of-function mutant lines expressing GFP-CaaL proteins, we demonstrated that Me ... The attenuation is achieved by adding a gene to the virus, which encodes a ballast protein. Production of the ballast protein ... Chlorophyll f-synthase (ChlF) is a D1 protein paralog. Modelling PSII-ChlF complexes determined several key protein motifs of ...
A chloroplast-localised fluorescent protein enhances the photosynthetic action spectrum in green algae. Day, A., 1 Sept 2022, ... Industrial and therapeutic proteins expressed in chloroplasts accumulate to extraordinarily high levels providing an attractive ... For example, pharmaceutical proteins, and proteins conferring herbicide and insect resistance. We are also transforming ... Biotechnology and Molecular Biology of Chloroplasts. Chloroplasts are members of the plastid family of organelles found in ...
  • Protein-specific energy requirements for protein transport across or into thylakoid membranes. (
  • Integral membrane proteins within both the stromal and granal membranes are therefore highly constrained, possibly forming 'microdomains' that are sharply separated. (
  • Nagy and Pogany, 2008b ), and RNA replication is done by viral proteins and host plant proteins in chloroplast membranes of the infected cell. (
  • While the former are commonly found in the bacterial inner membrane and cell membranes of all eukaryotic cells, the latter are located exclusively in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria ( Cavalier-Smith, 2000 ). (
  • John E. Walker The ATP synthases are multiprotein complexes found in the energy-transducing membranes of bacteria, chloroplasts and mitochondria. (
  • Christoph Benning Plant chloroplasts contain an intricate photosynthetic membrane system, the thylakoids, and are surrounded by two envelope membranes at which thylakoid lipids are assembled. (
  • These pigments are embedded in the membranes of the chloroplast in groups called photosystems. (
  • In chloroplasts, TAT is involved in transporting folded proteins across the membranes of THYLAKOIDS. (
  • Mounting evidence suggests that the genetic disorders/mutation and diseases change not only the protein expression patterns but also membranes themselves. (
  • Reactive oxygen species (ROS)-dependent signaling pathways from chloroplasts and mitochondria merge at the nuclear protein RADICAL-INDUCED CELL DEATH1 (RCD1). (
  • Thus, RCD1 integrates organellar signaling from chloroplasts and mitochondria to establish transcriptional control over the metabolic processes in both organelles. (
  • These signalling events often involve multiple cellular organelles including mitochondria, chloroplasts, plasma membrane and the endoplasmic reticulum. (
  • They equipped the nuclei of the two wild species N. benthamiana and N. glauca with genes that encoded a resistance to an antibiotic as well as the yellow fluorescent protein The cultivated tobacco, on the other hand, had chloroplasts that carried genes coding for a resistance to another antibiotic and a green fluorescent protein. (
  • 1998 - 1999 Expression of nuclear genes for chloroplast ribosomal proteins. (
  • variegata by down regulating the transcription of 28 chloroplast genes and disturbing chloroplast biogenesis and thylakoid membrane development. (
  • RNA-Seq revealed that 28 chloroplast genes (cpDEGs) were all down-regulated in YSs, of which, four involved in chloroplast protein translation and 21 of photosynthesis system (PS)I, PSII, cytochrome b6/f complex and ATP synthase are crucial for chloroplast biogenesis/development. (
  • This process requires the extensive exchange of lipid precursors between the chloroplast and the ER (endoplasmic reticulum). (
  • The protein is thus either immobile within the thylakoid membrane, or its diffusion is tightly restricted within distinct regions. (
  • 2010 ) have reputed that one signal is sufficient for the stepwise transport of two distinct passenger proteins across the thylakoid membrane. (
  • MSc Azfar Ali Bajwa defends the dissertation in Molecular Plant Biology titled "DIVERSITY IN PHOSPHORYLATION OF THYLAKOID MEMBRANE PROTEINS IN CHLOROPLASTS" at the University of Turku on 09 April 2024 at 12.00 (University of Turku, Main building, Säästöpankki lecture hall, Turku). (
  • Specifically, I found that a specific protein called CURT1B, and its phosphorylation, contributes to the fine-tuning of thylakoid membrane ultrastructure and function in response to different light conditions. (
  • Chloroplast thylakoid membrane-stabilised emulsions. (
  • The stabilisation mechanism can be described as a combined effect of surface-active molecules, mainly membrane proteins but also membrane lipids, exposed on surfaces of thylakoid membrane vesicles adsorbed as particles. (
  • OMPdb ( ) was introduced as a database for β-barrel outer membrane proteins from Gram-negative bacteria in 2011 and then included 69,354 entries classified into 85 families. (
  • Integral membrane proteins (IMPs) play a vital role in cell tasks and communication. (
  • They can be structurally divided into two distinct categories, the α-helical membrane proteins and the β-barrel ones ( von Heijne, 1999 ). (
  • one order of magnitude lower than that of α-helical membrane proteins). (
  • However, the β-barrel membrane proteins participate in crucial biological activities in prokaryotic organisms, as well as in the eukaryotic organelles. (
  • OMPdb is a database of bacterial β-barrel outer membrane proteins (βOMPs). (
  • While the identification of novel intracellular channels and transporters - as well as the characterization of their structures and mechanisms - continues to produce exciting discoveries, new insights as emerging regarding the regulation of these membrane proteins which enable their roles to be elucidated in the context of the dynamic nature of organelles and the wider roles played by organellar channels and transporters in cellular and organismal homeostasis. (
  • Microalgae have potential as platforms for the synthesis of high-value recombinant proteins due to their many beneficial attributes including ease of cultivation, lack of pathogenic agents, and low-cost downstream processing. (
  • The mannosyltransferase Och1 is the key enzyme for synthesis of elaborated protein N-glycans in yeast. (
  • RNA-binding proteins (RBPs) regulate RNA processing steps from synthesis to decay, including pre-mRNA splicing, transport, 3′ end formation, translation, and degradation. (
  • Researchers believe these findings will help scientists further understand of evolution and breeding of new plant varieties since the new chloroplast genome can be handed down to the next generation plants. (
  • The new chloroplast genome can even be handed down to the next generation and, thereby, give a plant new traits. (
  • Due to the nature of the experiment, it would have to be cells from N. benthamiana or N. glauca that acquired chloroplasts, or the chloroplast genome, from N. tabacum. (
  • We found a completely identical version of the chloroplast genome from N. tabacum in the two other species. (
  • However, the lack of a genome-wide view of their in vivo binding targets and binding landscapes represents a gap in understanding the mode of action of plant RNA-binding proteins. (
  • Here, we adapt individual nucleotide resolution crosslinking and immunoprecipitation (iCLIP) genome-wide to determine the binding repertoire of the circadian clock-regulated Arabidopsis thaliana glycine-rich RNA-binding protein At GRP7. (
  • Arabidopsis thaliana harbors 197 proteins with an RNA recognition motif (RRM), the most frequent type of RNA-binding domain [ 1 ]. (
  • In a first RIP-seq analysis in Arabidopsis , more than 4000 targets of the serine/arginine rich (SR)-like protein SR45 were identified by RNA immunoprecipitation, followed by high-throughput sequencing [ 5 ]. (
  • My thesis explores the regulation of photosynthesis through protein phosphorylations, mainly by thylakoid-associated protein kinases, both in a moss (Physcomitrium patens, an early land plant) and in an angiosperm (Arabidopsis thaliana, a flowering plant model species). (
  • Arabidopsis research explored the dynamics and phosphorylation of photosynthetic proteins under changing light conditions, in comparison to that occurring in Physcomitrella. (
  • Both RNA polymerase PEP and NEP coexist in seed-plant chloroplasts and the ßâ ³ subunit of PEP is encoded by rpoC2. (
  • Specific and non-specific diffusion channels, together with biogenesis/secretion proteins have a crucial role in the bacterial life. (
  • Hydrogenases, formate dehydrogenases and several non-redox proteins (about two dozen in E. coli ), including virulence factors, periplasmic binding proteins, and enzymes involved in envelope biogenesis, have the 'twin R' motif and probably use this pathway. (
  • The chloroplast is a vital organelle of plant cells carrying out photosynthesis. (
  • My research identifies new targets for studying photosynthesis and shows how calcium and protein phosphorylation co-operate in chloroplasts. (
  • Higher-order multi-protein complexes such as RNA polymerase II (Pol II) complexes with transcription initiation factors are often not amenable to X-ray structure determination. (
  • The chaperone cycle of heat shock protein-90 (Hsp90) involves progression through defined complexes with different cochaperones. (
  • Additionally, I discovered that calcium signaling, along with thylakoid protein phosphorylations, modulates the key proteins involved in the repair of thylakoid protein complexes. (
  • These viruses have small genomes that encode a limited number of proteins. (
  • A transfer of chloroplasts genomes can occur in contact zones between plants. (
  • They tried to explain this phenomenon, for which they coined the term "chloroplast capture" with the assumption that every once in a while those normally sexually incompatible species crossed and produced offspring with a new combination of nuclear and chloroplast genomes. (
  • Now, scientists around Ralph Bock from the Max Planck Institute of Molecular Plant Physiology in Potsdam discovered that a transfer of entire chloroplasts, or at least their genomes, can occur in contact zones between plants. (
  • Sexually incompatible species can exchange chloroplast genomes at graft sites. (
  • Protein translocase in BACTERIA or CHLOROPLASTS that exports or secretes folded proteins. (
  • In GRAM-NEGATIVE BACTERIA, twin-arginine translocase (TAT) is involved in the export of folded proteins to the PERIPLASM. (
  • Accumulating MDS gene products, including alternative oxidases (AOXs), affect redox status of the chloroplasts, leading to changes in chloroplast ROS processing and increased protection of photosynthetic apparatus. (
  • Changing light conditions together with other environmental stresses may severely damage the photosynthetic apparatus in chloroplasts. (
  • Here, we present the upgrade of OMPdb, which from now on aims to become a global repository for all transmembrane β-barrel proteins, both eukaryotic and bacterial. (
  • TatE embarks at the transmembrane helix five of TatC where it becomes so closely spaced to TatB that both proteins can be covalently linked by a zero-space cross-linker. (
  • In 2009, Ralph Bock and Sandra Stegemann discovered that genetic information stored in the green chloroplasts can be transferred to another plant by means of horizontal gene transfer. (
  • The present mini-review first describes the technique of cryo-ET and then discusses its role in membrane bioenergetics specifically in chloroplasts and mitochondrial. (
  • Small heat shock proteins (sHSPs) have been shown to play a role in the molecular response to 1O2. (
  • However, knowledge of molecular mechanisms and functions underlying these chloroplast host factors during the virus infection is still scarce and remains largely unknown. (
  • She is an MSc student currently working in the Woodson lab on plastid localized small heat shock proteins and their involvement in singlet oxygen response and signaling. (
  • Notably, I found that the formation of a moss-specific PSI Large protein complex relies on the phosphorylation of specific LHCBM proteins by the STN7 kinase. (
  • Recently researchers have reported that chloroplast proteins are crucial for replicating (+)ss plant RNA viruses. (
  • Therefore, chloroplasts play central roles in replicating several plant virus species and biosynthesis of most plant hormones, making chloroplast factors crucial for plant defense response. (
  • I gained evolutionary insights into kinases, such as STN7 and STN8, and their target proteins, and discovered that mosses employ a distinct strategy to avoid excessive sunlight compared to flowering plants. (
  • ROS alter the abundance, thiol redox state and oligomerization of the RCD1 protein in vivo, providing feedback control on its function. (
  • To date, global mapping of in vivo RNA-protein interactions is performed by immunopurification of RNA-binding proteins using antibodies against the native protein or an epitope, and cataloguing the associated RNAs by RNA-seq. (
  • To preserve the physiological RNA-protein interactions, RNA and bound proteins are often crosslinked in vivo. (
  • In contrast, other chloroplast proteins such as PAP2.1, PSaC, and ATPsyn-α play active roles in plant defense against viruses. (
  • Our review briefly summarizes the latest knowledge regarding the possible role of chloroplast in plant virus replication, emphasizing chloroplast-related proteins. (
  • We have highlighted current advances regarding chloroplast-related proteins' role in replicating plant (+)ss RNA viruses. (
  • Plant scientists were confounded by the fact that the DNA extracted from the plants' green chloroplasts sometimes showed the greatest similarities when related species grew in the same area. (
  • Functions for RNA-binding proteins in orchestrating plant development and environmental responses are well established. (
  • Typical plant cell chloroplast approx. (
  • In enzymology, a chloroplast protein-transporting ATPase (EC is an enzyme that catalyzes the chemical reaction ATP + H2O ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. (
  • The systematic name of this enzyme class is ATP phosphohydrolase (chloroplast protein-importing). (
  • IspG protein serves as the penultimate enzyme of the recently discovered non-mevalonate pathway for the biosynthesis of the universal isoprenoid precursors, isopentenyl diphosphate and dimethylallyl diphosphate. (
  • RCD1-dependent regulation is linked to chloroplast signaling by 3'-phosphoadenosine 5'-phosphate (PAP). (
  • The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in protein sequences. (
  • View conserved domains detected in this protein sequence using CD-search. (
  • Using a genetics approach, we have shown that sHSPs may protect chloroplastic proteins during medium to extreme photooxidative stress. (
  • Knowing how individual chloroplasts communicate and mitigate stress can not only help us further understand interorganelle signaling, but can also provide insight into photosynthetic flux and thus further inform future crop engineering and farming practices. (
  • We used these transformant lines to study the effect of temperature, light and media on recombinant protein production and cell growth. (
  • These proteins associate with their cofactors in the cell cytoplasm before translocation. (
  • A systematic comparison between mRNA and protein displayed emerging expression patterns of key therapeutic targets (CD274, YAP1, AKT1, and CDH1). (
  • Any process in which a protein is maintained in a specific location a specific location on or in an organelle, and is prevented from moving elsewhere. (
  • However, current recombinant protein levels are low compared to other microbial platforms and stable insertion of transgenes is available in only a few microalgal species. (
  • This is also consistent with the idea that reactive oxygen species, salicylic acid, jasmonic acid, and abscisic acid are produced in chloroplast. (