Ribosomes: Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Escherichia coli: 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.Ribosomal Proteins: Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits.Ribosome Subunits, Small, Bacterial: The small subunit of eubacterial RIBOSOMES. It is composed of the 16S RIBOSOMAL RNA and about 23 different RIBOSOMAL PROTEINS.Peptide Chain Initiation, Translational: A process of GENETIC TRANSLATION whereby the formation of a peptide chain is started. It includes assembly of the RIBOSOME components, the MESSENGER RNA coding for the polypeptide to be made, INITIATOR TRNA, and PEPTIDE INITIATION FACTORS; and placement of the first amino acid in the peptide chain. The details and components of this process are unique for prokaryotic protein biosynthesis and eukaryotic protein biosynthesis.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.RNA, Bacterial: Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.Codon, Initiator: A codon that directs initiation of protein translation (TRANSLATION, GENETIC) by stimulating the binding of initiator tRNA (RNA, TRANSFER, MET). In prokaryotes, the codons AUG or GUG can act as initiators while in eukaryotes, AUG is the only initiator codon.Molecular Sequence Data: 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.RNA, Ribosomal: The most abundant form of RNA. Together with proteins, it forms the ribosomes, playing a structural role and also a role in ribosomal binding of mRNA and tRNAs. Individual chains are conventionally designated by their sedimentation coefficients. In eukaryotes, four large chains exist, synthesized in the nucleolus and constituting about 50% of the ribosome. (Dorland, 28th ed)RNA, Messenger: 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.5' Untranslated Regions: The sequence at the 5' end of the messenger RNA that does not code for product. This sequence contains the ribosome binding site and other transcription and translation regulating sequences.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Ribosome Subunits: The two dissimilar sized ribonucleoprotein complexes that comprise a RIBOSOME - the large ribosomal subunit and the small ribosomal subunit. The eukaryotic 80S ribosome is composed of a 60S large subunit and a 40S small subunit. The bacterial 70S ribosome is composed of a 50S large subunit and a 30S small subunit.RNA, Transfer: The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.Ribosome Subunits, Large, Bacterial: The large subunit of the eubacterial 70s ribosome. It is composed of the 23S RIBOSOMAL RNA, the 5S RIBOSOMAL RNA, and about 37 different RIBOSOMAL PROTEINS.Ribosome Subunits, Large, Eukaryotic: The large subunit of the 80s ribosome of eukaryotes. It is composed of the 28S RIBOSOMAL RNA, the 5.8S RIBOSOMAL RNA, the 5S RIBOSOMAL RNA, and about 50 different RIBOSOMAL PROTEINS.Codon: A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).Peptide Initiation Factors: Protein factors uniquely required during the initiation phase of protein synthesis in GENETIC TRANSLATION.Peptide Chain Elongation, Translational: A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.RNA, Transfer, Amino Acyl: Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Operon: In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.Bacterial Proteins: Proteins found in any species of bacterium.Ribosome Subunits, Small, Eukaryotic: The small subunit of the 80s ribosome of eukaryotes. It is composed of the 18S RIBOSOMAL RNA and 32 different RIBOSOMAL PROTEINS.Amino Acid Sequence: 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.Polyribosomes: A multiribosomal structure representing a linear array of RIBOSOMES held together by messenger RNA; (RNA, MESSENGER); They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Genes, Bacterial: The functional hereditary units of BACTERIA.Ribosome Inactivating Proteins, Type 1: Ribosome inactivating proteins consisting of only the toxic A subunit, which is a polypeptide of around 30 kDa.Peptide Chain Termination, Translational: A process of GENETIC TRANSLATION whereby the terminal amino acid is added to a lengthening polypeptide. This termination process is signaled from the MESSENGER RNA, by one of three termination codons (CODON, TERMINATOR) that immediately follows the last amino acid-specifying CODON.Cloning, Molecular: 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.Peptide Elongation Factor G: Peptide Elongation Factor G catalyzes the translocation of peptidyl-tRNA from the A to the P site of bacterial ribosomes by a process linked to hydrolysis of GTP to GDP.Mutation: 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.RNA, Transfer, Met: A transfer RNA which is specific for carrying methionine to sites on the ribosomes. During initiation of protein synthesis, tRNA(f)Met in prokaryotic cells and tRNA(i)Met in eukaryotic cells binds to the start codon (CODON, INITIATOR).Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Anticodon: The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome.Protein Binding: 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.Reticulocytes: Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes.RNA Caps: Nucleic acid structures found on the 5' end of eukaryotic cellular and viral messenger RNA and some heterogeneous nuclear RNAs. These structures, which are positively charged, protect the above specified RNAs at their termini against attack by phosphatases and other nucleases and promote mRNA function at the level of initiation of translation. Analogs of the RNA caps (RNA CAP ANALOGS), which lack the positive charge, inhibit the initiation of protein synthesis.Prokaryotic Initiation Factor-3: A prokaryotic initiation factor that plays a role in recycling of ribosomal subunits for a new round of translational initiation. It binds to 16S RIBOSOMAL RNA and stimulates the dissociation of vacant 70S ribosomes. It may also be involved in the preferential binding of initiator tRNA to the 30S initiation complex.RNA-Binding Proteins: Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.Host Factor 1 Protein: An integration host factor that was originally identified as a bacterial protein required for the integration of bacteriophage Q beta (ALLOLEVIVIRUS). Its cellular function may be to regulate mRNA stability and processing in that it binds tightly to poly(A) RNA and interferes with ribosome binding.Puromycin: A cinnamamido ADENOSINE found in STREPTOMYCES alboniger. It inhibits protein synthesis by binding to RNA. It is an antineoplastic and antitrypanosomal agent and is used in research as an inhibitor of protein synthesis.Peptide Termination Factors: Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.RNA, Viral: Ribonucleic acid that makes up the genetic material of viruses.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Eukaryotic Initiation Factor-3: A multisubunit eukaryotic initiation factor that contains at least 8 distinct polypeptides. It plays a role in recycling of ribosomal subunits to the site of transcription initiation by promoting the dissociation of non-translating ribosomal subunits. It also is involved in promoting the binding of a ternary complex of EUKARYOTIC INITIATION FACTOR-2; GTP; and INITIATOR TRNA to the 40S ribosomal subunit.Carmovirus: A genus in the family TOMBUSVIRIDAE mostly found in temperate regions. Some species infecting legumes (FABACEAE) are reported from tropical areas. Most viruses are soil-borne, but some are transmitted by the fungus Olpidium radicale and others by beetles. Carnation mottle virus is the type species.Poly U: A group of uridine ribonucleotides in which the phosphate residues of each uridine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Ribonucleases: Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-.Peptide Elongation Factors: Protein factors uniquely required during the elongation phase of protein synthesis.Eukaryotic Initiation Factor-4F: A trimeric peptide initiation factor complex that associates with the 5' MRNA cap structure of RNA (RNA CAPS) and plays an essential role in MRNA TRANSLATION. It is composed of EUKARYOTIC INITIATION FACTOR-4A; EUKARYOTIC INITIATION FACTOR-4E; and EUKARYOTIC INITIATION FACTOR-4G.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.RNA, Small Untranslated: Short RNA, about 200 base pairs in length or shorter, that does not code for protein.Genes: A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.Cell-Free System: A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)Eukaryotic Initiation Factor-4A: A component of eukaryotic initiation factor 4F that as an RNA helicase involved in unwinding the secondary structure of the 5' UNTRANSLATED REGION of MRNA. The unwinding facilitates the binding of the 40S ribosomal subunit.RNA Processing, Post-Transcriptional: Post-transcriptional biological modification of messenger, transfer, or ribosomal RNAs or their precursors. It includes cleavage, methylation, thiolation, isopentenylation, pseudouridine formation, conformational changes, and association with ribosomal protein.Endoribonucleases: A family of enzymes that catalyze the endonucleolytic cleavage of RNA. It includes EC 3.1.26.-, EC 3.1.27.-, EC 3.1.30.-, and EC 3.1.31.-.Kinetics: The rate dynamics in chemical or physical systems.Signal Recognition Particle: A cytosolic ribonucleoprotein complex that acts to induce elongation arrest of nascent presecretory and membrane proteins until the ribosome becomes associated with the rough endoplasmic reticulum. It consists of a 7S RNA and at least six polypeptide subunits (relative molecular masses 9, 14, 19, 54, 68, and 72K).beta-Galactosidase: A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS, GM1.RNA, Antisense: RNA molecules which hybridize to complementary sequences in either RNA or DNA altering the function of the latter. Endogenous antisense RNAs function as regulators of gene expression by a variety of mechanisms. Synthetic antisense RNAs are used to effect the functioning of specific genes for investigative or therapeutic purposes.RNA: A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Ribosome Subunits, Small: The small ribonucleoprotein component of RIBOSOMES. It contains the MESSENGER RNA binding site and two TRANSFER RNA binding sites - one for the incoming AMINO ACYL TRNA (A site) and the other (P site) for the peptidyl tRNA carrying the elongating peptide chain.RNA Stability: The extent to which an RNA molecule retains its structural integrity and resists degradation by RNASE, and base-catalyzed HYDROLYSIS, under changing in vivo or in vitro conditions.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.RNA, Ribosomal, 23S: Constituent of 50S subunit of prokaryotic ribosomes containing about 3200 nucleotides. 23S rRNA is involved in the initiation of polypeptide synthesis.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Protein Sorting Signals: Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.Open Reading Frames: A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Peptide Biosynthesis: The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.Peptide Elongation Factor Tu: A protein found in bacteria and eukaryotic mitochondria which delivers aminoacyl-tRNA's to the A site of the ribosome. The aminoacyl-tRNA is first bound to a complex of elongation factor Tu containing a molecule of bound GTP. The resulting complex is then bound to the 70S initiation complex. Simultaneously the GTP is hydrolyzed and a Tu-GDP complex is released from the 70S ribosome. The Tu-GTP complex is regenerated from the Tu-GDP complex by the Ts elongation factor and GTP.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Membrane Proteins: 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.Lac Operon: The genetic unit consisting of three structural genes, an operator and a regulatory gene. The regulatory gene controls the synthesis of the three structural genes: BETA-GALACTOSIDASE and beta-galactoside permease (involved with the metabolism of lactose), and beta-thiogalactoside acetyltransferase.Triticum: A plant genus of the family POACEAE that is the source of EDIBLE GRAIN. A hybrid with rye (SECALE CEREALE) is called TRITICALE. The seed is ground into FLOUR and used to make BREAD, and is the source of WHEAT GERM AGGLUTININS.Centrifugation, Density Gradient: Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Peptidylprolyl Isomerase: An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.Protein Structure, Tertiary: 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.Promoter Regions, Genetic: DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.Cryoelectron Microscopy: Electron microscopy involving rapid freezing of the samples. The imaging of frozen-hydrated molecules and organelles permits the best possible resolution closest to the living state, free of chemical fixatives or stains.Molecular Weight: The sum of the weight of all the atoms in a molecule.Eukaryotic Initiation Factor-4E: A peptide initiation factor that binds specifically to the 5' MRNA CAP STRUCTURE of MRNA in the CYTOPLASM. It is a component of the trimeric complex EIF4F.Ribosome Subunits, Large: The largest ribonucleoprotein component of RIBOSOMES. It contains the domains which catalyze formation of the peptide bond and translocation of the ribosome along the MESSENGER RNA during GENETIC TRANSLATION.Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Thiostrepton: One of the CYCLIC PEPTIDES from Streptomyces that is active against gram-positive bacteria. In veterinary medicine, it has been used in mastitis caused by gram-negative organisms and in dermatologic disorders.DNA Restriction Enzymes: Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1.Recombinant Fusion Proteins: 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.Ricin: A protein phytotoxin from the seeds of Ricinus communis, the castor oil plant. It agglutinates cells, is proteolytic, and causes lethal inflammation and hemorrhage if taken internally.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.RNA, Ribosomal, 28S: Constituent of the 60S subunit of eukaryotic ribosomes. 28S rRNA is involved in the initiation of polypeptide synthesis in eukaryotes.Codon, Terminator: Any codon that signals the termination of genetic translation (TRANSLATION, GENETIC). PEPTIDE TERMINATION FACTORS bind to the stop codon and trigger the hydrolysis of the aminoacyl bond connecting the completed polypeptide to the tRNA. Terminator codons do not specify amino acids.Thermus thermophilus: A species of gram-negative, aerobic, rod-shaped bacteria found in hot springs of neutral to alkaline pH, as well as in hot-water heaters.Bacteriophage lambda: A temperate inducible phage and type species of the genus lambda-like viruses, in the family SIPHOVIRIDAE. Its natural host is E. coli K12. Its VIRION contains linear double-stranded DNA with single-stranded 12-base 5' sticky ends. The DNA circularizes on infection.Cell Nucleolus: Within most types of eukaryotic CELL NUCLEUS, a distinct region, not delimited by a membrane, in which some species of rRNA (RNA, RIBOSOMAL) are synthesized and assembled into ribonucleoprotein subunits of ribosomes. In the nucleolus rRNA is transcribed from a nucleolar organizer, i.e., a group of tandemly repeated chromosomal genes which encode rRNA and which are transcribed by RNA polymerase I. (Singleton & Sainsbury, Dictionary of Microbiology & Molecular Biology, 2d ed)RNA, Ribosomal, 16S: Constituent of 30S subunit prokaryotic ribosomes containing 1600 nucleotides and 21 proteins. 16S rRNA is involved in initiation of polypeptide synthesis.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Poliovirus: A species of ENTEROVIRUS which is the causal agent of POLIOMYELITIS in humans. Three serotypes (strains) exist. Transmission is by the fecal-oral route, pharyngeal secretions, or mechanical vector (flies). Vaccines with both inactivated and live attenuated virus have proven effective in immunizing against the infection.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.RNA, Transfer, Phe: A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.Genetic Engineering: Directed modification of the gene complement of a living organism by such techniques as altering the DNA, substituting genetic material by means of a virus, transplanting whole nuclei, transplanting cell hybrids, etc.Peptide Elongation Factor 2: Peptide Elongation Factor 2 catalyzes the translocation of peptidyl-tRNA from the A site to the P site of eukaryotic ribosomes by a process linked to the hydrolysis of GTP to GDP.GTP Phosphohydrolase-Linked Elongation Factors: Factors that utilize energy from the hydrolysis of GTP to GDP for peptide chain elongation. EC 3.6.1.-.Intracellular Membranes: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Oligonucleotides: Polymers made up of a few (2-20) nucleotides. In molecular genetics, they refer to a short sequence synthesized to match a region where a mutation is known to occur, and then used as a probe (OLIGONUCLEOTIDE PROBES). (Dorland, 28th ed)Sequence Alignment: 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.Peptidyl Transferases: Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.DNA, Recombinant: Biologically active DNA which has been formed by the in vitro joining of segments of DNA from different sources. It includes the recombination joint or edge of a heteroduplex region where two recombining DNA molecules are connected.RNA, Ribosomal, 18S: Constituent of the 40S subunit of eukaryotic ribosomes. 18S rRNA is involved in the initiation of polypeptide synthesis in eukaryotes.Viral Proteins: Proteins found in any species of virus.Genes, Viral: The functional hereditary units of VIRUSES.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Fusidic Acid: An antibiotic isolated from the fermentation broth of Fusidium coccineum. (From Merck Index, 11th ed). It acts by inhibiting translocation during protein synthesis.Genetic Vectors: DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition.Base Composition: The relative amounts of the PURINES and PYRIMIDINES in a nucleic acid.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.Sparsomycin: An antitumor antibiotic produced by Streptomyces sparsogenes. It inhibits protein synthesis in 70S and 80S ribosomal systems.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Models, Genetic: Theoretical representations that simulate the behavior or activity of genetic processes or phenomena. They include the use of mathematical equations, computers, and other electronic equipment.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Regulatory Sequences, Nucleic Acid: Nucleic acid sequences involved in regulating the expression of genes.Chloramphenicol: An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106)Bacteriophages: Viruses whose hosts are bacterial cells.Binding, Competitive: The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Paromomycin: An oligosaccharide antibiotic produced by various STREPTOMYCES.Dogs: The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)Viomycin: A strongly basic peptide, antibiotic complex from several strains of Streptomyces. It is allergenic and toxic to kidneys and the labyrinth. Viomycin is used in tuberculosis as several different salts and in combination with other agents.RNA, Fungal: Ribonucleic acid in fungi having regulatory and catalytic roles as well as involvement in protein synthesis.Genes, Reporter: Genes whose expression is easily detectable and therefore used to study promoter activity at many positions in a target genome. In recombinant DNA technology, these genes may be attached to a promoter region of interest.Bacterial Outer Membrane Proteins: Proteins isolated from the outer membrane of Gram-negative bacteria.Protein Synthesis Inhibitors: Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins.Repressor Proteins: Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.Magnesium: A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.Dihydrostreptomycin Sulfate: A semi-synthetic aminoglycoside antibiotic that is used in the treatment of TUBERCULOSIS.Cell Fractionation: Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.DNA Transposable Elements: Discrete segments of DNA which can excise and reintegrate to another site in the genome. Most are inactive, i.e., have not been found to exist outside the integrated state. DNA transposable elements include bacterial IS (insertion sequence) elements, Tn elements, the maize controlling elements Ac and Ds, Drosophila P, gypsy, and pogo elements, the human Tigger elements and the Tc and mariner elements which are found throughout the animal kingdom.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Frameshifting, Ribosomal: A directed change in translational READING FRAMES that allows the production of a single protein from two or more OVERLAPPING GENES. The process is programmed by the nucleotide sequence of the MRNA and is sometimes also affected by the secondary or tertiary mRNA structure. It has been described mainly in VIRUSES (especially RETROVIRUSES); RETROTRANSPOSONS; and bacterial insertion elements but also in some cellular genes.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Streptomycin: An antibiotic produced by the soil actinomycete Streptomyces griseus. It acts by inhibiting the initiation and elongation processes during protein synthesis.Endoplasmic Reticulum, Rough: A type of endoplasmic reticulum (ER) where polyribosomes are present on the cytoplasmic surfaces of the ER membranes. This form of ER is prominent in cells specialized for protein secretion and its principal function is to segregate proteins destined for export or intracellular utilization.Lincomycin: An antibiotic produced by Streptomyces lincolnensis var. lincolnensis. It has been used in the treatment of staphylococcal, streptococcal, and Bacteroides fragilis infections.Erythromycin: A bacteriostatic antibiotic macrolide produced by Streptomyces erythreus. Erythromycin A is considered its major active component. In sensitive organisms, it inhibits protein synthesis by binding to 50S ribosomal subunits. This binding process inhibits peptidyl transferase activity and interferes with translocation of amino acids during translation and assembly of proteins.Nucleic Acid Hybridization: Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503)DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Eukaryotic Initiation Factor-4G: A component of eukaryotic initiation factor-4F that is involved in multiple protein interactions at the site of translation initiation. Thus it may serve a role in bringing together various initiation factors at the site of translation initiation.RNA, Ribosomal, 5.8S: Constituent of the 60S subunit of eukaryotic ribosomes. 5.8S rRNA is involved in the initiation of polypeptide synthesis in eukaryotes.Picornaviridae: A family of small RNA viruses comprising some important pathogens of humans and animals. Transmission usually occurs mechanically. There are nine genera: APHTHOVIRUS; CARDIOVIRUS; ENTEROVIRUS; ERBOVIRUS; HEPATOVIRUS; KOBUVIRUS; PARECHOVIRUS; RHINOVIRUS; and TESCHOVIRUS.Microscopy, Electron: Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
Tejedor, F; Ballesta, JP (1986). "Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site ... thermic effect or thermic reaction may refer to a near-explosive property thermic reaction or thermic binding can refer to ...
2002). "Membrane-bound Ribosomes Define the Rough ER". Molecular Biology of the Cell 4th edition. Garland Science. Retrieved ... Many types of cells export proteins produced by ribosomes attached to the rough ER. The ribosomes assemble amino acids into ... It is a phase-dark body that is composed of an aggregation of membrane-bound vesicles containing cell wall components, serving ... As polypeptides intended to be membrane proteins grow from the ribosomes, they are inserted into the ER membrane itself and are ...
When the ribosome stalls at the 3'end of mRNA the tm-RNA is joined to the ribosome from the A site which has amino acid ... attached to it (11-amino acid tag). Then, the amino acid binds to the polypeptide chain. Then the normal translation will ... The non-stop decay pathway releases ribosomes that have reached the far 3' end of an mRNA and guides the mRNA to the exosome ... The non-stop decay pathway discharges the ribosomes that have stalled at the 3' end of mRNA and directs the mRNA to the exosome ...
... binds to the 30S subunit of microbial ribosomes. Thus, it prevents introduction of new amino acids to the nascent ... Ribosomal protection proteins interact with the ribosome and dislodge tetracycline from the ribosome, allowing for translation ... Tetracycline inhibits protein synthesis by blocking the attachment of charged aminoacyl-tRNA to the A site on the ribosome. ... Mammalian cells are less vulnerable to the effect of tetracyclines, despite the fact that tetracycline binds to the small ...
This prevents ribosomes from binding the gene's start codon. They are also found in the 5'UTR of htrA (high temperature ... Shine, J.; Dalgarno, L. (1975). "Determinant of cistron specificity in bacterial ribosomes". Nature. 254 (5495): 34-8. doi: ...
... this is known as reversible binding. Once attached completely, irreversible binding is initiated and the tail contracts, ... Within minutes, bacterial ribosomes start translating viral mRNA into protein. For RNA-based phages, RNA replicase is ... The bound, selected phages can be multiplied by reinfecting a susceptible bacterial strain, thus allowing them to retrieve the ... This specificity means a bacteriophage can infect only certain bacteria bearing receptors to which they can bind, which in turn ...
The function of the S4 domain is to be an RNA-binding protein. S4 is a multifunctional protein, and it must bind to the 16S ... Maguire BA, Zimmermann RA (March 2001). "The ribosome in focus". Cell. 104 (6): 813-6. doi:10.1016/s0092-8674(01)00278-1. PMID ... In molecular biology, S4 domain refers to a small RNA-binding protein domain found in a ribosomal protein named S4. The S4 ... Aravind L, Koonin EV (March 1999). "Novel predicted RNA-binding domains associated with the translation machinery". J. Mol. ...
Nou X, Kadner RJ (June 2000). "Adenosylcobalamin inhibits ribosome binding to btuB RNA". Proc. Natl. Acad. Sci. U.S.A. 97 (13 ... manganese riboswitches bind manganese ions. NiCo riboswitches bind the metal ions nickel and cobalt. PreQ1 riboswitches bind ... Riboswitch-mediated folding sequesters the ribosome-binding site, thereby inhibiting translation. The riboswitch is a ribozyme ... Purine riboswitches binds purines to regulate purine metabolism and transport. Different forms of the purine riboswitch bind ...
Piatyszek MA, Denslow ND, O'Brien TW (1988). "RNA binding proteins of the large subunit of bovine mitochondrial ribosomes". ... Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% ... Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among ... "The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present". J Biol ...
Ribosomes are most often identified by their sedimentation coefficient. For instance, the 70 S ribosome that comes from ... When two particles bind together, there is inevitably a loss of surface area. Thus, when measured separately they will have ... svedberg values that may not add up to that of the bound particle. This is notably the case with the ribosome. ...
The start codon is often preceded by a 5' untranslated region (5' UTR). In prokaryotes this includes the ribosome binding site ... The start codon is the first codon of a messenger RNA (mRNA) transcript translated by a ribosome. The start codon always codes ...
The binding of a charged initiator tRNA into the P site of the ribosome 3. The proper alignment of the ribosome with mRNA's ... The ribosome possesses three tRNA binding sites: the aminoacyl site (A site), the peptidyl site (P site), and the exit site (E ... The binding of the correct tRNA into the A site of the ribosome 2. The formation of a peptide bond between the tRNA in the A ... In addition to binding an amino acid, tRNA has a three nucleotide unit called an anticodon that base pairs with specific ...
DNA can sometimes occur as single strands (often needing to be stabilized by single-strand binding proteins) or as A-form or Z- ... Examples are tRNA, ribosomes, ribozymes, and riboswitches. These complex structures are facilitated by the fact that RNA ... Structured RNA molecules can do highly specific binding of other molecules and can themselves be recognized specifically; in ... or inhibitors bound. It is often important as an inactive storage, transport, or secretory form of a protein. This is required ...
The ribosome binds mRNA and carries out protein synthesis. Several ribosomes may be attached to a single mRNA at any time. ... The mRNA is then exported from the nucleus to the cytoplasm, where it is bound to ribosomes and translated into its ... In prokaryotic cells, which do not have nucleus and cytoplasm compartments, mRNA can bind to ribosomes while it is being ... Ribosomal RNA (rRNA) is the catalytic component of the ribosomes. Eukaryotic ribosomes contain four different rRNA molecules: ...
Milon P, Carotti M, Konevega AL, Wintermeyer W, Rodnina MV, Gualerzi CO (2010). "The ribosome-bound initiation factor 2 ... S11 and H45 are located near the Shine-Dalgarno binding site, which is also near the IF3 binding site. Proteins S3, S4, S5, and ... Pactamycin interrupts the binding in the Shine-Dalgarno binding region in the small subunit, thus disrupting activity. ... Once the 16S rRNA recognizes the mRNA start codon, a special tRNA, f-Met-tRNA binds and protein translation begins. The binding ...
55S RNP makes up ~75% of the nucleolar population of pre-ribosomes. To form mature rRNA 18S, 5.8S, and 28S, pre-rRNA 40S ( ... During transcription of pre-rRNA, early ribosomal binding proteins associate. It is thought that this 30S RNP containing 45S ... The Nucleolus and Ribosome Biogenesis. Vienna: Springer-Verlag KG. 1985 . Gerbi SA, Borovjagin AV. Pre-Ribosomal RNA Processing ... Nucleolin, an abundant phosphoprotein, binds to the pre-rRNA immediately after transcription and facilitates the base-pairing ...
The binding site of the ribosome on the rough endoplasmic reticulum is the translocon. However, the ribosomes are not a stable ... A ribosome only binds to the RER once a specific protein-nucleic acid complex forms in the cytosol. This special complex forms ... ISBN 0-7167-4366-3. Seiser, R. M. (2000). "The Fate of Membrane-bound Ribosomes Following the Termination of Protein Synthesis ... Ribosomes at this point may be released back into the cytosol; however, non-translating ribosomes are also known to stay ...
The tuberactinomycins target bacterial ribosomes, binding RNA and disrupting bacterial protein biosynthesis. It is produced by ... the actinomycete Streptomyces puniceus, that binds to RNA and inhibits prokaryotic protein synthesis and certain forms of RNA ...
1980: First demonstration of the binding of a chaperone to a newly synthesised polypeptide. 1987: Formulation of the general ... 1973: First identification of a product of protein synthesis by chloroplast ribosomes. 1978: First demonstration of in vitro ...
This process accomplishes the inhibition of ribosomes binding to host cell mRNAs. This effectively shuts down cap-dependent ... Riabi, 2014) When VP1 binds to the Coxsackie-Adenovirus receptor (CAR), which can be found on heart muscle cells as well as ...
This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for ... It promotes the GTP-dependent translocation of the ribosome. This protein is completely inactivated by EF-2 kinase ... "Kinetic determination of the effects of ADP-ribosylation on the interaction of eukaryotic elongation factor 2 with ribosomes". ...
The ribosome has three sites for tRNA to bind. They are the aminoacyl site (abbreviated A), the peptidyl site (abbreviated P) ... The ribosome facilitates decoding by inducing the binding of complementary tRNA anticodon sequences to mRNA codons. The tRNAs ... In prokaryotes (bacteria), translation occurs in the cytoplasm, where the large and small subunits of the ribosome bind to the ... Instead, the stop codon induces the binding of a release factor protein that prompts the disassembly of the entire ribosome/ ...
Upon GTP binding, both Gα-GTP and Gβγ separate from both the receptor and from each other. Depending on the lifetime of the ... Protein biosynthesis (a.k.a. translation) at the ribosome. Control and differentiation during cell division. Translocation of ... On binding with the complex, GDP dissociates from the complex; the receptor works as a GEF - GDP-GTP Exchange Factor; the free ... Toggling the switch is performed by the unidirectional change of the GTPase from the active, GTP-bound form to the inactive, ...
Effects of Chloramphenicol Upon a Ribosomal Amino Acid Polymerization System and Its Binding to Bacterial Ribosome". Biochimica ... The acetylation prevents chloramphenicol from binding to the ribosome. Resistance-conferring mutations of the 50S ribosomal ... It specifically binds to A2451 and A2452 residues in the 23S rRNA of the 50S ribosomal subunit, preventing peptide bond ... Chloramphenicol bound to proteins in the PDB MedlinePlus DrugInfo uspdi-202125 Pharmacy and pharmacology portal Medicine portal ...
This yields a modified RNA strand which cannot be read by the ribosomes. It is a pale yellow, odorless, crystalline powder. ... through inhibition of the GTP-binding protein (G protein) Rac1, which regulates the Rac/Vav pathway. An additional effect may ...
Once released into the blood and lymph, these antibody molecules bind to the target antigen (foreign substance) and initiate ... Other organelles in a plasma cell include ribosomes, lysosomes, mitochondria, and the plasma membrane. ... These T cells bind to the MHC II-antigen molecule and cause activation of the B cell. This is a type of safeguard to the system ... by selection for the ability to bind antigen with higher affinity, the activation and growth of B cell clones able to secrete ...
Owing to structural constraints, EF-G appears unable to simultaneously bind to FusB-type proteins and the ribosome. Based on ... in which FusB-type proteins drive the release of frozen FA-EF-G-GDP complexes from the ribosome by competing for binding to EF- ... The protein-protein interaction occurs away from the FA binding site of EF-G, suggesting that FusB-type proteins do not mediate ... Instead, FusB-type proteins interact with the portion of EF-G known to make contact with the inside of the ribosome. ...
SAP is a powerful ribosome-inactivating protein isolated from the seeds of the plant Saponaria officinalis.13 It has been used ... Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc Natl Acad Sci U S A. ... Killing of K562 cells with conjugates between human transferrin and a ribosome-inactivating protein (SO-6). Br J Haematol. 1988 ... Stirpe F, Barbieri L. Ribosome-inactivating proteins up to date. FASEB Lett. 1986;195:1-8. ...
... acetylation of the antibiotic catalysed by the enzyme and the failure of the 3-acetoxy product to bind to bacterial ribosomes. ... Further binding studies with fusidate analogues, including bile salts, have shown some of the structural constraints on the ... Steady-state kinetic studies with the type I enzyme have shown that the binding of fusidic acid is competitive with respect to ... support the data from in vitro experiments to give a coherent mechanism for fusidic acid resistance based on reversible binding ...
Binds to 50S ribosomes unit and suppresses bacterial protein synthesis.. Bile is an important means of excretion appeared the ...
Ribosomes at the end of the psaA ORF remain bound to the membrane after ribonuclease treatment, whereas ribosomes at the start ... Bacterial SecA is bound to the ribosome (38) and could potentially bind signal sequences cotranslationally. Assays similar to ... Recent analyses of ribosome profiling data have revealed mRNA-programmed ribosome pauses that enhance SRP binding and faithful ... S1), indicating that initiating ribosomes are not bound to the membrane. However, elongating ribosomes relocate to the membrane ...
... it is not considered a ribosome binding site. Eukaryotic ribosomes are known to bind to transcripts in a mechanism unlike the ... A ribosome binding site, or ribosomal binding site, (RBS) is a sequence of nucleotides upstream of the start codon of an mRNA ... 9] Sequences within ribosome binding site affecting messenger RNA translatability and method to direct ribosomes to single ... "Ribosomal Binding Site Sequence Requirements". www.thermofisher.com. Retrieved 2015-10-16. "Help:Ribosome Binding Site - parts. ...
The alpha operon ribosome binding site in bacteria is surrounded by this complex pseudoknotted RNA structure. Translation of ... Page for Alpha operon ribosome binding site at Rfam. ... acts as a translational repressor by binding to the nested ... The mechanism of repression is thought to involve a conformational switch in the pseudoknot region and ribosome entrapment. ...
... it is not considered a ribosome binding site.[2][8] Internal ribosome entry site (IRES)[edit]. Eukaryotic ribosomes are known ... A ribosome binding site, or ribosomal binding site (RBS), is a sequence of nucleotides upstream of the start codon of an mRNA ... 9] Sequences within ribosome binding site affecting messenger RNA translatability and method to direct ribosomes to single ... "Ribosome binding site recognition using neural networks". Genetics and Molecular Biology. 27 (4): 644-650. doi:10.1590/S1415- ...
Murthy M.R.V. (1970) Membrane-Bound and Free Ribosomes in the Developing Rat Brain. In: Lajtha A. (eds) Protein Metabolism of ... Sucrose Density Gradient Free Ribosome Amino Acid Incorporation Ribonucleoprotein Particle Brain Microsome These keywords were ...
Binding of Ribosomes to btuB RNA Requires a Ribosome-Associated Factor(s).. Ribosome subunits prepared with the usual high-salt ... Methyl-Cbl inhibited ribosome binding at a 10-fold higher concentration. The inhibition of ribosome binding by methyl-Cbl ... was used to detect the binding of ribosomes to btuB mRNA. This assay measures the ability of a bound ribosome to block ... the inhibition of ribosome binding is less than expected for translation-level control. Substantial ribosome binding was also ...
ribosome-binding protein 1. Names. 180 kDa ribosome receptor homolog. ES/130-related protein. ribosome binding protein 1 ... RRBP1 ribosome binding protein 1 [Homo sapiens] RRBP1 ribosome binding protein 1 [Homo sapiens]. Gene ID:6238 ... Rib_recp_KP_reg; Ribosome receptor lysine/proline rich region. * NM_001365613.2 → NP_001352542.1 ribosome-binding protein 1 ... ribosome binding protein 1provided by HGNC. Primary source. HGNC:HGNC:10448 See related. Ensembl:ENSG00000125844 MIM:601418 ...
... and spoke with them about their work on internal ribosome entry, and the requirement for a cellular microRNA for hepatitis C ...
ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. Does not hydrolyze ... ATP-binding, Magnesium, Metal-binding, Nucleotide-binding. Enzyme and pathway databases. BioCyc Collection of Pathway/Genome ... ribosome binding Source: EcoCyc ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function, process ... Ribosome-binding ATPase YchFUniRule annotation. ,p>Manual validated information which has been generated by the UniProtKB ...
Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug ...
... from the GTP-bound to the GDP-bound state involves substantial conformational changes of IF2 and of the entire ribosome. In the ... IF2 is a GTPase essential for binding initiator transfer RNA to the 30S ribosomal subunit and recruiting the 50S subunit into ... whereas in the GDP-bound state IF2 steps back and adopts a ready-to-leave conformation. Our data also provide insights into ... GTP analog-bound state, IF2 interacts mostly with the 30S subunit and extends to the initiator tRNA in the peptidyl (P) site, ...
The structure of a release factor bound to an RNA stop codon shows which amino acids form the binding site for U in the first ... The structure of a release factor bound to an RNA stop codon shows which amino acids form the binding site for U in the first ... Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome ... Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome ...
We therefore asked if the role of RACK1 in translation depends on its binding to the ribosome or on a ribosome-independent ... R36D K38E mutant RACK1 does not bind ribosomes efficiently. (A) Ribosome profiles coupled with Western blots show the ... whereas the addition of a RACK1 mutant that is unable to bind ribosomes does not. Outside the ribosome, RACK1 has a reduced ... Affinity grid-based cryo-EM of PKC binding to RACK1 on the ribosome. J Struct Biol 181:190-194. doi:10.1016/j.jsb.2012.11.006. ...
... Tobin, Christina Uppsala University, ... ribosome, protein synthesis, ribosomal proteins, translation initiation, ribosome biogenesis, fitness costs, compensatory ... 1. Removal and Replacement of Ribosomal Proteins: Effects on Bacterial Fitness and Ribosome Function. Open this publication in ... This clearly demonstrates the robustness and plasticity of the ribosome and protein synthesis in general and it also implies ...
The structure of EF-P bound to the ribosome. (A) Overview of the E- and P-site tRNAs bound to the 70S ribosome [coordinates ... EF-P does not bind to the ribosome in a classical tRNA-binding site, but rather binds at a distinct position that is adjacent ... EF-P binds to the 70S ribosome at a site located between the binding sites for the peptidyl tRNA (P site) and the exiting tRNA ... Portions of the 70S ribosome were omitted for clarity. (B) Overview of EF-P and P-site tRNA-binding in the 70S ribosome. The 50 ...
Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA. Sujata S. Jha1, ... Jha, S. S., Komar, A. A. Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along ... To isolate nascent polypeptide bound to ribosomes (polysome), translation reaction is layered on top of 4.5 ml of 30% glycerol ... An alternative protocol based on selective isolation of translating ribosomes bound to a biotin-labeled mRNA has been also ...
Binding of ribosomes to yeast PK-RM and Sec61 proteoliposomes. (A-C) Scatchard plots of ribosome binding to PK-RM (A and B) or ... Ribosome binding to yeast PK-RM, Sec61 proteoliposomes, or Sec61 heterotrimers. Ribosomes were isolated from wild-type yeast as ... in ribosome-binding affinity caused by several L8 sec61 mutations was accompanied by an apparent increase in ribosome binding ... Δ strain bind ribosomes in a saturable manner (Fig. 6 A, closed circles), with a binding affinity (Kd = 5.5 ± 0.5 nM) that is ...
In all organisms, initiation of translation depends on molecular recognition of the messenger RNA by ribosomes. In prokaryotes ...
Prevention, by ribosome-bound nascent polyphenylalanine chains, of the functional interaction of t-2 toxin with its receptor ... Competition experiments between verrucarin A and [3H]anisomycin indicated that verrucarin A bound to run off ribosomes from ... 4. Studies were also carried out with yeast run off ribosomes prepared from both a wild-type strain and a strain resistant to ... 2. [acetyl-14C]Trichodermin bound to yeast polyribosomes with a dissociation constant of 2.10 muM and to yeast run off ...
Here, we report that human ribosome-binding factor A (RBFA) is a mitochondrial RNA-binding protein that exerts crucial roles in ... ribosome-binding and RNA-binding KH domains. The basic residues (in bold) Arg7, Arg10, Arg45, Arg80, Lys85 and Arg90 in E. ... ribosome-binding and RNA-binding KH domains, which in the human protein are predicted to lie in the central portion (amino ... The human RNA-binding protein RBFA promotes the maturation of the mitochondrial ribosome. Agata Rozanska, Ricarda Richter- ...
  • Determinations of antibiotic resistance levels and estimates of intracellular chloramphenicol acetyltransferase concentrations support the data from in vitro experiments to give a coherent mechanism for fusidic acid resistance based on reversible binding of the antibiotic to the enzyme. (le.ac.uk)
  • Further binding studies with fusidate analogues, including bile salts, have shown some of the structural constraints on the steroidal skeleton of the ligand which are necessary for binding to the enzyme. (le.ac.uk)
  • 4V7S: Crystal structure of the E. coli ribosome bound to telithromycin. (rcsb.org)
  • Virtual reality demonstration showing antibiotic bound to E coli ribosome (PDB 4v7s) for reception after Byer's Award Lecture given by Danica Fujimori on "Unlocking the Mystery of Antibiotic Resistance", Tuesday January 31, 4:30 PM. Reception is in Genentech Hall atrium where HTC Vive demo will be set up for public viewing. (ucsf.edu)
  • Show E. coli ribosome with telithromycin antibiotic bound (residue name TEL), PDB 4v7s , a 2010 structure from the Jamie Cate lab at UC Berkeley. (ucsf.edu)
  • E. coli continues to serve as a key model for the structure and function of the ribosome, structures of ribosome from other organisms and domains of life have also greatly contributed to our knowledge of protein synthesis. (asmscience.org)
  • Creative Biolabs provides E. coli S30 cell-free lysate for ribosome display, either with coupled or uncoupled transcription and translation. (creative-biolabs.com)
  • In gram-negative bacteria like E. coli the version of this protein resides near the core of the ribosome. (weizmann.ac.il)
  • We discuss the properties of the overlapping gene in relation to its lysis function, recognition of the lysis initiator region by E. coli versus eucaryotic ribosomes and op3 as a ribosome binding site mutant for the f2 synthetase cistron. (cshl.edu)
  • The average ribosome of E. coli , the best-characterized example, measures about 200 angstroms (about 20 nm) in diameter. (britannica.com)
  • Here, we show that elongation factor G (EF-G) triggers ribosome take-off by a pseudotranslocation event using a small mRNA stem-loop as an A-site transfer RNA mimic and requires hydrolysis of about two molecules of guanosine 5′-triphosphate per nucleotide of the noncoding gap. (sciencemag.org)
  • The first study, in Proceedings of the National Academy of Sciences, concerns the intimate signaling between the ribosome and an elongation factor (EF-Tu) that is essential to the successful assembly of a growing protein. (innovations-report.com)
  • Features in the nascent peptide that underlie these distinct behaviors were revealed by analysis of the position on each mRNA at which elongating ribosomes first become attached to the membrane. (pnas.org)
  • The transition from soluble to membrane-attached ribosomes occurs shortly after the first transmembrane segment in the nascent peptide has emerged from the ribosome. (pnas.org)
  • For identification of specific peptides that interact and inhibit the stalled-ribosome rescues, peptide aptamer library (pTRG-SN-peptides) was constructed using pTRG as vector and Staphylococcus aureus nuclease (SN) as scaffold protein, in which 16 random amino acids were introduced to form an exposed surface loop. (frontiersin.org)
  • Thus, the engineered A. veronii C4 conferring PA-2 expression might be potentially attenuated vaccine, and also the peptide aptamer PA-2 could develop as anti-microbial drugs targeted to the ribosome rescued factors in A. veronii . (frontiersin.org)
  • In bacteria, the first chaperone that interacts with nascent peptide chains is trigger factor (TF), a 48-kDa protein that binds to ribosomes at 1:1 stoichiometry with moderate affinity (5-7). (lw90.com)
  • Both TF and SRP bind to the ribosome in the vicinity of the peptide exit, and crosslinking experiments have revealed ribosomal protein L23 as a common attachment site (9-11). (lw90.com)
  • Whereas SRP binding to RNCs is Distinguishedly promoted by the signal sequence, TF probably binds to any nascent peptide, with some preference for sequences containing aromatic amino acids (12). (lw90.com)
  • This is the active site, where the important business of the ribosome takes place (e.g. peptide bond formation). (coursehero.com)
  • During the termination phase, the fully synthesized peptide is released from the ribosome for posttranslational processing. (asnjournals.org)
  • This gives researchers a very detailed image of the components of the ribosome, but offers no clues about its behavior when it encounters other molecules. (innovations-report.com)
  • In the scene, ribbons show RNA, spheres show protein components of the ribosome, and the transparent surface near the ligand shows the experimental X-ray data used to determine this structure. (ucsf.edu)
  • How defects in ribosomes, the essential organelles required for protein biosynthesis in all cells, cause tissue-specific abnormalities in human disease remains a question of fundamental scientific and medical importance. (bloodjournal.org)
  • Translation of the genetically encoded information into polypeptides, protein biosynthesis, is a central function executed by ribosomes in all cells. (europa.eu)
  • Accurate assembly and maturation of human mitochondrial ribosomes is essential for synthesis of the 13 polypeptides encoded by the mitochondrial genome. (biochemj.org)
  • Mitochondrial ribosomes differ between species [ 3 , 8 - 11 ] but for mammalian mitoribosome assembly, as with the eubacterial system, the number of key assembly factors is likely to be few [ 12 - 17 ]. (biochemj.org)
  • The structure shows details of stop-codon recognition by RF2, as well as interactions of RF2 with the PTC and other regions of the ribosome including helix 69 (H69) and the L11 region. (pubmedcentralcanada.ca)
  • The subsequent codon is stop codon UAG ( Fig. 1A ), but instead of terminating protein synthesis, the ribosome slides over a 50-nucleotide (nt)-long noncoding gap, lands at a distal GGA codon, and resumes translation to the end of the second ORF. (sciencemag.org)
  • RHF promotes and stabilizes dimerization of 70S ribosomes by the ribosome modulation factor (RMF), leading to the formation of inactive 100S ribosomes during the stationary phase [ PMID: 18174192 ]. (ebi.ac.uk)
  • Here, we present the first full 70S ribosome structure from Staphylococcus aureus, a Gram-positive pathogenic bacterium, solved by cryo-electron microscopy. (nih.gov)