Group II Chaperonins
Group I Chaperonins
Chaperonin Containing TCP-1
t-Complex Genome Region
Molecular Sequence Data
Amino Acid Sequence
HSP70 Heat-Shock Proteins
Sequence Homology, Amino Acid
Protein Structure, Tertiary
p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function. (1/963)Genetic screens in Drosophila have identified p50(cdc37) to be an essential component of the sevenless receptor/mitogen-activated kinase protein (MAPK) signaling pathway, but neither the function nor the target of p50(cdc37) in this pathway has been defined. In this study, we examined the role of p50(cdc37) and its Hsp90 chaperone partner in Raf/Mek/MAPK signaling biochemically. We found that coexpression of wild-type p50(cdc37) with Raf-1 resulted in robust and dose-dependent activation of Raf-1 in Sf9 cells. In addition, p50(cdc37) greatly potentiated v-Src-mediated Raf-1 activation. Moreover, we found that p50(cdc37) is the primary determinant of Hsp90 recruitment to Raf-1. Overexpression of a p50(cdc37) mutant which is unable to recruit Hsp90 into the Raf-1 complex inhibited Raf-1 and MAPK activation by growth factors. Similarly, pretreatment with geldanamycin (GA), an Hsp90-specific inhibitor, prevented both the association of Raf-1 with the p50(cdc37)-Hsp90 heterodimer and Raf-1 kinase activation by serum. Activation of Raf-1 via baculovirus coexpression with oncogenic Src or Ras in Sf9 cells was also strongly inhibited by dominant negative p50(cdc37) or by GA. Thus, formation of a ternary Raf-1-p50(cdc37)-Hsp90 complex is crucial for Raf-1 activity and MAPK pathway signaling. These results provide the first biochemical evidence for the requirement of the p50(cdc37)-Hsp90 complex in protein kinase regulation and for Raf-1 function in particular. (+info)
Enhanced fatty streak formation in C57BL/6J mice by immunization with heat shock protein-65. (2/963)Recent data suggest that the immune system is involved in atherogenesis. Thus, interest has been raised as to the possible antigens that could serve as the initiators of the immune reaction. In the current work, we studied the effects of immunization with recombinant heat shock protein-65 (HSP-65) and HSP-65-rich Mycobacterium tuberculosis (MT) on early atherogenesis in C57BL/6J mice fed either a normal chow diet or a high-cholesterol diet (HCD). A rapid, cellular immune response to HSP-65 was evident in mice immunized with HSP-65 or with MT but not in the animals immunized with phosphate-buffered saline (PBS) alone. Early atherosclerosis was significantly enhanced in HCD-fed mice immunized with HSP-65 (n=10; mean aortic lesion size, 45 417+/-9258 microm2) or MT (n=15; 66 350+/-6850 microm2) compared with PBS-injected (n=10; 10 028+/-3599 microm2) or nonimmunized (n=10; 9500+/-2120 microm2) mice. No fatty streak lesions were observed in mice fed a chow diet regardless of the immunization protocol applied. Immunohistochemical analysis of atherosclerotic lesions from the HSP-65- and MT-immunized mice revealed infiltration of CD4 lymphocytes compared with the relatively lymphocyte-poor lesions in the PBS-treated or nonimmunized mice. Direct immunofluorescence analysis of lesions from HSP-65- and MT-immunized mice fed an HCD exhibited extensive deposits of immunoglobulins compared with the fatty streaks in the other study groups, consistent with the larger and more advanced lesions found in the former 2 groups. This model, which supports the involvement of HSP-65 in atherogenesis, furnishes a valuable tool to study the role of the immune system in atherogenesis. (+info)
Identification of Mycobacterium kansasii by using a DNA probe (AccuProbe) and molecular techniques. (3/963)The newly formulated Mycobacterium kansasii AccuProbe was evaluated, and the results obtained with the new version were compared to the results obtained with the old version of this test by using 116 M. kansasii strains, 1 Mycobacterium gastri strain, and 19 strains of several mycobacterial species. The sensitivity of this new formulation was 97.4% and the specificity was 100%. Still, three M. kansasii strains were missed by this probe. To evaluate the variability within the species, genetic analyses of the hsp65 gene, the spacer sequence between the 16S and 23S rRNA genes, and the 16S rRNA gene of several M. kansasii AccuProbe-positive strains as well as all AccuProbe-negative strains were performed. Genetic analyses of the one M. gastri strain from the comparative assay and of two further M. gastri strains were included because of the identity of the 16S rRNA gene in M. gastri to that in M. kansasii. The data confirmed the genetic heterogeneity of M. kansasii. Furthermore, a subspecies with an unpublished hsp65 restriction pattern and spacer sequence was described. The genetic data indicate that all M. kansasii strains missed by the AccuProbe test belong to one subspecies, the newly described subspecies VI, as determined by the hsp65 restriction pattern and the spacer sequence. Since the M. kansasii strains that are missed are rare and all M. gastri strains are correctly negative, the new formulated AccuProbe provides a useful tool for the identification of M. kansasii. (+info)
Endothelial cytotoxicity mediated by serum antibodies to heat shock proteins of Escherichia coli and Chlamydia pneumoniae: immune reactions to heat shock proteins as a possible link between infection and atherosclerosis. (4/963)BACKGROUND: Growing evidence suggests that an immunological reaction against heat shock proteins (HSPs) may be involved in atherogenesis. Because HSPs show a high degree of amino acid sequence homology between different species, from prokaryotes to humans, we investigated the possibility of "antigenic mimicry" caused by an immunological cross-reaction between microorganisms and autoantigens. METHODS AND RESULTS: Serum antibodies against the Escherichia coli HSP (GroEL) and the 60-kDa chlamydial HSP (cHSP60) from subjects with atherosclerosis were purified by use of affinity chromatography. Western blot analyses and competitive ELISAs confirmed the cross-reaction of the eluted antibodies with human HSP60 and the bacterial counterparts. The cytotoxicity of anti-GroEL and anti-cHSP60 antibodies was determined on human endothelial cells labeled with 51Cr. A significant difference (40% versus 8%) was observed in the specific 51Cr release of heat-treated (42 degrees C for 30 minutes) and untreated cells, respectively, in the presence of these anti-HSP antibodies and complement. This effect was blocked by addition of 100 microg/mL recombinant GroEL. In addition, seropositivity against specific non-HSP60 Chlamydia pneumoniae antigens is more prominent among high-anti-HSP titer sera than low-titer sera. CONCLUSIONS: Serum antibodies against HSP65/60 cross-react with human HSP60, cHSP60, and GroEL; correlate with the presence of antibodies to C pneumoniae and endotoxin; and mediate endothelial cytotoxicity. These findings suggest that humoral immune reactions to bacterial HSPs, such as cHSP60 and GroEL, may play an important role in the process of vascular endothelial injury, which is believed to be a key event in the pathogenesis of atherosclerosis. (+info)
Isolation and characterization of a second subunit of molecular chaperonin from Pyrococcus kodakaraensis KOD1: analysis of an ATPase-deficient mutant enzyme. (5/963)The cpkA gene encoding a second (alpha) subunit of archaeal chaperonin from Pyrococcus kodakaraensis KOD1 was cloned, sequenced, and expressed in Escherichia coli. Recombinant CpkA was studied for chaperonin functions in comparison with CpkB (beta subunit). The effect on decreasing the insoluble form of proteins was examined by coexpressing CpkA or CpkB with CobQ (cobyric acid synthase from P. kodakaraensis) in E. coli. The results indicate that both CpkA and CpkB effectively decrease the amount of the insoluble form of CobQ. Both CpkA and CpkB possessed the same ATPase activity as other bacterial and eukaryal chaperonins. The ATPase-deficient mutant proteins CpkA-D95K and CpkB-D95K were constructed by changing conserved Asp95 to Lys. Effect of the mutation on the ATPase activity and CobQ solubilization was examined. Neither mutant exhibited ATPase activity in vitro. Nevertheless, they decreased the amount of the insoluble form of CobQ by coexpression as did wild-type CpkA and CpkB. These results implied that both CpkA and CpkB could assist protein folding for nascent protein in E. coli without requiring energy from ATP hydrolysis. (+info)
GroEL/GroES-dependent reconstitution of alpha2 beta2 tetramers of humanmitochondrial branched chain alpha-ketoacid decarboxylase. Obligatory interaction of chaperonins with an alpha beta dimeric intermediate. (6/963)The decarboxylase component (E1) of the human mitochondrial branched chain alpha-ketoacid dehydrogenase multienzyme complex (approximately 4-5 x 10(3) kDa) is a thiamine pyrophosphate-dependent enzyme, comprising two 45.5-kDa alpha subunits and two 37.8-kDa beta subunits. In the present study, His6-tagged E1 alpha2 beta2 tetramers (171 kDa) denatured in 8 M urea were competently reconstituted in vitro at 23 degrees C with an absolute requirement for chaperonins GroEL/GroES and Mg-ATP. Unexpectedly, the kinetics for the recovery of E1 activity was very slow with a rate constant of 290 M-1 s-1. Renaturation of E1 with a similarly slow kinetics was also achieved using individual GroEL-alpha and GroEL-beta complexes as combined substrates. However, the beta subunit was markedly more prone to misfolding than the alpha in the absence of GroEL. The alpha subunit was released as soluble monomers from the GroEL-alpha complex alone in the presence of GroES and Mg-ATP. In contrast, the beta subunit discharged from the GroEL-beta complex readily rebound to GroEL when the alpha subunit was absent. Analysis of the assembly state showed that the His6-alpha and beta subunits released from corresponding GroEL-polypeptide complexes assembled into a highly structured but inactive 85.5-kDa alpha beta dimeric intermediate, which subsequently dimerized to produce the active alpha2 beta2 tetrameter. The purified alpha beta dimer isolated from Escherichia coli lysates was capable of binding to GroEL to produce a stable GroEL-alpha beta ternary complex. Incubation of this novel ternary complex with GroES and Mg-ATP resulted in recovery of E1 activity, which also followed slow kinetics with a rate constant of 138 M-1 s-1. Dimers were regenerated from the GroEL-alpha beta complex, but they needed to interact with GroEL/GroES again, thereby perpetuating the cycle until the conversion from dimers to tetramers was complete. Our study describes an obligatory role of chaperonins in priming the dimeric intermediate for subsequent tetrameric assembly, which is a slow step in the reconstitution of E1 alpha2 beta2 tetramers. (+info)
Cloning, sequencing and molecular analysis of the Campylobacter jejuni groESL bicistronic operon. (7/963)The groESL bicistronic operon from the enteric pathogen Campylobacter jejuni was cloned and sequenced. It consists of two ORFs encoding proteins with molecular masses of 9.5 and 57.9 kDa, which showed a high degree of homology to other bacterial GroES and GroEL proteins. Northern blot analysis suggested that the groESL operon is transcribed as a bicistronic mRNA, and its steady-state level was markedly increased after temperature upshift. By primer extension assay, one potential transcription start point preceding the groESL genes could be demonstrated, and a putative promoter region compatible with both Escherichia coli and C. jejuni sigma70 consensus sequences was identified. A conserved inverted repeat, which is believed to be involved in the regulation of the groESL genes, was found between the -10 promoter box and the groES translation start site. The complete coding region of groEL was fused with pET-22b(+) and expressed in E. coli as a His6-tagged recombinant protein (rCjHsp60-His). After purification, the protein was recognized by an anti-HSP60 monoclonal antibody. ELISA and Western immunoblotting experiments showed that IgG and IgA antibody responses against rCjHsp60-His were not significantly increased in sera from 24 patients with sporadic Campylobacter infection when compared to sera from 16 healthy controls. (+info)
Chaperone-mediated protein folding. (8/963)The folding of most newly synthesized proteins in the cell requires the interaction of a variety of protein cofactors known as molecular chaperones. These molecules recognize and bind to nascent polypeptide chains and partially folded intermediates of proteins, preventing their aggregation and misfolding. There are several families of chaperones; those most involved in protein folding are the 40-kDa heat shock protein (HSP40; DnaJ), 60-kDa heat shock protein (HSP60; GroEL), and 70-kDa heat shock protein (HSP70; DnaK) families. The availability of high-resolution structures has facilitated a more detailed understanding of the complex chaperone machinery and mechanisms, including the ATP-dependent reaction cycles of the GroEL and HSP70 chaperones. For both of these chaperones, the binding of ATP triggers a critical conformational change leading to release of the bound substrate protein. Whereas the main role of the HSP70/HSP40 chaperone system is to minimize aggregation of newly synthesized proteins, the HSP60 chaperones also facilitate the actual folding process by providing a secluded environment for individual folding molecules and may also promote the unfolding and refolding of misfolded intermediates. (+info)
Chaperonins are a class of molecular chaperones that assist in the folding of proteins. They are found in all forms of life and play a crucial role in maintaining cellular homeostasis by preventing protein aggregation and misfolding. There are two main types of chaperonins: Group I chaperonins, which are found in the cytoplasm, and Group II chaperonins, which are found in the mitochondria and chloroplasts. The most well-known chaperonin is the GroEL/GroES complex, which is found in Group I chaperonins. This complex consists of two subunits, GroEL and GroES, which work together to fold proteins. GroEL acts as a cage-like structure that surrounds the unfolded protein, while GroES acts as a lid that covers the opening of the cage. The two subunits work together to facilitate the folding of the protein by providing a protected environment and using ATP to drive conformational changes in the protein. Chaperonins are important for the proper functioning of many cellular processes, including protein synthesis, cell division, and stress response. Mutations in chaperonin genes can lead to a variety of diseases, including neurodegenerative disorders, such as Alzheimer's and Parkinson's disease, and certain types of cancer.
Group II chaperonins are a class of molecular chaperones that are found in the cytosol of eukaryotic cells and in the cytoplasm and chloroplasts of plant cells. They are also present in some prokaryotic cells. These chaperonins are composed of two stacked rings of protein subunits, with each ring consisting of multiple copies of the same subunit. The subunits are arranged in a way that creates a central cavity, which is where the substrate proteins are folded and unfolded. Group II chaperonins are involved in the folding of a wide variety of proteins, including enzymes, structural proteins, and membrane proteins. They function by binding to unfolded or partially folded proteins and using the energy from ATP hydrolysis to facilitate their proper folding. This process is thought to occur in a protected environment within the central cavity of the chaperonin, which shields the substrate protein from potentially damaging interactions with other cellular components. Group II chaperonins are also involved in the folding of proteins that are involved in the assembly of larger complexes, such as ribosomes and the cytoskeleton. In these cases, the chaperonin may help to bring together multiple subunits of the complex and facilitate their proper assembly. Group II chaperonins are important for the proper functioning of cells, as they play a critical role in the folding of many proteins that are essential for cellular processes. Mutations in the genes encoding group II chaperonins have been linked to a number of human diseases, including neurodegenerative disorders and certain types of cancer.
Chaperonin 10, also known as CCT or TRiC, is a large, multisubunit protein complex that plays a crucial role in the folding of newly synthesized proteins in the cell. It is composed of two rings of seven subunits each, with a central cavity that allows proteins to enter and fold within the complex. The chaperonin 10 complex is found in all eukaryotic cells and some bacteria, and it is essential for the proper folding of many proteins, particularly those that are difficult to fold on their own. It works by providing a protected environment for proteins to fold, preventing misfolding and aggregation that can lead to protein damage or disease. Disruptions in the function of chaperonin 10 have been linked to a number of diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease, as well as certain types of cancer. Understanding the role of chaperonin 10 in protein folding and its potential as a therapeutic target is an active area of research in the medical field.
Chaperonin 60, also known as GroEL or Hsp60, is a protein complex that plays a crucial role in the folding and assembly of proteins in the cell. It is found in all organisms, from bacteria to humans, and is particularly important in the folding of newly synthesized proteins and the refolding of misfolded proteins. The chaperonin 60 complex consists of two identical subunits, each with a molecular weight of approximately 60 kDa, hence the name. The subunits form a barrel-like structure with a central cavity that can accommodate unfolded or partially folded proteins. The complex uses energy from ATP hydrolysis to facilitate the folding process by stabilizing the intermediate states of the protein as it folds into its final structure. In the medical field, chaperonin 60 has been implicated in a number of diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease, as well as certain types of cancer. Abnormal folding of chaperonin 60 has also been linked to the development of certain types of bacterial infections. As such, understanding the role of chaperonin 60 in protein folding and its involvement in disease may lead to the development of new therapeutic strategies for these conditions.
Group I chaperonins are a class of molecular chaperones that are found in all domains of life, including bacteria, archaea, and eukaryotes. They are large, multisubunit protein complexes that function to assist in the folding of newly synthesized polypeptides, as well as the refolding of misfolded proteins. Group I chaperonins are composed of two stacked rings of protein subunits, with the inner ring forming a hydrophobic cavity that is thought to provide a protected environment for the folding of polypeptides. The outer ring of the chaperonin contains ATPase activity, which is thought to drive the conformational changes that allow the polypeptide to fold properly. Group I chaperonins play an important role in maintaining cellular protein homeostasis and are involved in a number of cellular processes, including protein synthesis, protein degradation, and the assembly of large macromolecular complexes.
Chaperonin-containing TCP-1 (CCT) is a protein complex that plays a crucial role in the folding of newly synthesized proteins in the cell. It is composed of multiple subunits that form a barrel-like structure, and it is found in all cellular compartments, including the cytoplasm, mitochondria, and chloroplasts. CCT acts as a molecular chaperone, assisting in the folding of proteins by preventing them from aggregating and misfolding. It does this by binding to nascent polypeptide chains as they emerge from the ribosome and helping to fold them into their correct three-dimensional structure. CCT also plays a role in the assembly of multi-subunit proteins, such as ribosomes and proteasomes. Disruptions in the function of CCT have been linked to a number of human diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease, as well as certain types of cancer. Understanding the role of CCT in protein folding and its involvement in disease is an active area of research in the medical field.
I'm sorry, but I couldn't find any information on "Thermosomes" in the medical field. It's possible that you may have misspelled the term or that it is not a commonly used term in medicine. Can you please provide more context or information about where you heard or read about "Thermosomes"? This may help me to provide a more accurate response.
Thiosulfate Sulfurtransferase (TST) is an enzyme that plays a role in the metabolism of sulfur-containing compounds in the body. It is primarily found in the liver and is involved in the detoxification of various toxic compounds, including drugs and environmental pollutants. TST catalyzes the transfer of a sulfur atom from thiosulfate to a variety of substrates, including aromatic compounds, aliphatic compounds, and other sulfur-containing molecules. This reaction is an important step in the metabolism of many sulfur-containing compounds, and defects in TST activity can lead to the accumulation of toxic intermediates in the body. In the medical field, TST is often studied in the context of drug metabolism and detoxification, as well as in the treatment of certain liver diseases and disorders. It is also being investigated as a potential target for the development of new drugs for the treatment of cancer and other diseases.
Archaeal proteins are proteins that are encoded by the genes of archaea, a group of single-celled microorganisms that are distinct from bacteria and eukaryotes. Archaeal proteins are characterized by their unique amino acid sequences and structures, which have been the subject of extensive research in the field of biochemistry and molecular biology. In the medical field, archaeal proteins have been studied for their potential applications in various areas, including drug discovery, biotechnology, and medical diagnostics. For example, archaeal enzymes have been used as biocatalysts in the production of biofuels and other valuable chemicals, and archaeal proteins have been explored as potential targets for the development of new antibiotics and other therapeutic agents. In addition, archaeal proteins have been used as diagnostic markers for various diseases, including cancer and infectious diseases. For example, certain archaeal proteins have been found to be overexpressed in certain types of cancer cells, and they have been proposed as potential biomarkers for the early detection and diagnosis of these diseases. Overall, archaeal proteins represent a rich source of novel biological molecules with potential applications in a wide range of fields, including medicine.
Malate dehydrogenase (MDH) is an enzyme that plays a crucial role in cellular metabolism. It catalyzes the conversion of malate, a four-carbon compound, to oxaloacetate, a five-carbon compound, in the citric acid cycle. This reaction is reversible and can occur in both directions, depending on the cellular needs and the availability of energy. In the medical field, MDH is often studied in the context of various diseases and disorders. For example, mutations in the MDH gene have been associated with certain forms of inherited metabolic disorders, such as Leigh syndrome and MELAS (mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes). In addition, MDH has been implicated in the development of certain types of cancer, such as breast and prostate cancer, and may play a role in the progression of these diseases. Overall, MDH is an important enzyme in cellular metabolism and its dysfunction can have significant implications for human health.
Heat-shock proteins (HSPs) are a group of proteins that are produced in response to cellular stress, such as heat, oxidative stress, or exposure to toxins. They are also known as stress proteins or chaperones because they help to protect and stabilize other proteins in the cell. HSPs play a crucial role in maintaining cellular homeostasis and preventing the aggregation of misfolded proteins, which can lead to cell damage and death. They also play a role in the immune response, helping to present antigens to immune cells and modulating the activity of immune cells. In the medical field, HSPs are being studied for their potential as diagnostic and therapeutic targets in a variety of diseases, including cancer, neurodegenerative disorders, and infectious diseases. They are also being investigated as potential biomarkers for disease progression and as targets for drug development.
In the medical field, Archaea are a group of single-celled microorganisms that are distinct from bacteria and eukaryotes. They are found in a wide range of environments, including extreme environments such as hot springs, salt flats, and deep-sea hydrothermal vents. Archaea are known for their unique cell structures and metabolic processes. They have cell walls made of a different type of polymer than bacteria, and they often have a more complex metabolism that allows them to survive in harsh environments. In medicine, Archaea are of interest because some species are pathogenic and can cause infections in humans and animals. For example, Methanococcus voltae has been isolated from human infections, and some species of Archaea are associated with chronic infections in animals. Additionally, Archaea are being studied for their potential use in biotechnology. Some species are able to produce useful compounds, such as enzymes and biofuels, and they are being investigated as potential sources of new antibiotics and other therapeutic agents.
Adenosine triphosphatases (ATPases) are a group of enzymes that hydrolyze adenosine triphosphate (ATP) to adenosine diphosphate (ADP) and inorganic phosphate (Pi). These enzymes play a crucial role in many cellular processes, including energy production, muscle contraction, and ion transport. In the medical field, ATPases are often studied in relation to various diseases and conditions. For example, mutations in certain ATPase genes have been linked to inherited disorders such as myopathy and neurodegenerative diseases. Additionally, ATPases are often targeted by drugs used to treat conditions such as heart failure, cancer, and autoimmune diseases. Overall, ATPases are essential enzymes that play a critical role in many cellular processes, and their dysfunction can have significant implications for human health.
Molecular chaperones are a class of proteins that assist in the folding, assembly, and transport of other proteins within cells. They play a crucial role in maintaining cellular homeostasis and preventing the accumulation of misfolded or aggregated proteins, which can lead to various diseases such as neurodegenerative disorders, cancer, and certain types of infections. Molecular chaperones function by binding to nascent or partially folded proteins, preventing them from aggregating and promoting their proper folding. They also assist in the assembly of multi-subunit proteins, such as enzymes and ion channels, by ensuring that the individual subunits are correctly folded and assembled into a functional complex. There are several types of molecular chaperones, including heat shock proteins (HSPs), chaperonins, and small heat shock proteins (sHSPs). HSPs are induced in response to cellular stress, such as heat shock or oxidative stress, and are involved in the refolding of misfolded proteins. Chaperonins, on the other hand, are found in the cytosol and the endoplasmic reticulum and are involved in the folding of large, complex proteins. sHSPs are found in the cytosol and are involved in the stabilization of unfolded proteins and preventing their aggregation. Overall, molecular chaperones play a critical role in maintaining protein homeostasis within cells and are an important target for the development of new therapeutic strategies for various diseases.
Adenosine triphosphate (ATP) is a molecule that serves as the primary energy currency in living cells. It is composed of three phosphate groups attached to a ribose sugar and an adenine base. In the medical field, ATP is essential for many cellular processes, including muscle contraction, nerve impulse transmission, and the synthesis of macromolecules such as proteins and nucleic acids. ATP is produced through cellular respiration, which involves the breakdown of glucose and other molecules to release energy that is stored in the bonds of ATP. Disruptions in ATP production or utilization can lead to a variety of medical conditions, including muscle weakness, fatigue, and neurological disorders. In addition, ATP is often used as a diagnostic tool in medical testing, as levels of ATP can be measured in various bodily fluids and tissues to assess cellular health and function.
Bacterial proteins are proteins that are synthesized by bacteria. They are essential for the survival and function of bacteria, and play a variety of roles in bacterial metabolism, growth, and pathogenicity. Bacterial proteins can be classified into several categories based on their function, including structural proteins, metabolic enzymes, regulatory proteins, and toxins. Structural proteins provide support and shape to the bacterial cell, while metabolic enzymes are involved in the breakdown of nutrients and the synthesis of new molecules. Regulatory proteins control the expression of other genes, and toxins can cause damage to host cells and tissues. Bacterial proteins are of interest in the medical field because they can be used as targets for the development of antibiotics and other antimicrobial agents. They can also be used as diagnostic markers for bacterial infections, and as vaccines to prevent bacterial diseases. Additionally, some bacterial proteins have been shown to have therapeutic potential, such as enzymes that can break down harmful substances in the body or proteins that can stimulate the immune system.
Ribulose-1,5-bisphosphate carboxylase (RuBisCO) is an enzyme that plays a central role in the process of photosynthesis in plants, algae, and some bacteria. It catalyzes the reaction between carbon dioxide and ribulose-1,5-bisphosphate (RuBP), a 5-carbon sugar, to form two molecules of 3-phosphoglycerate (3-PGA), a 3-carbon compound. This reaction is the first step in the Calvin cycle, which is the primary pathway for carbon fixation in photosynthesis. RuBisCO is the most abundant enzyme on Earth and is responsible for fixing approximately 60% of the carbon dioxide in the atmosphere. However, it is also a slow enzyme and is often limited by the availability of carbon dioxide in the environment. This can lead to a phenomenon known as photorespiration, in which RuBisCO instead catalyzes the reaction between RuBP and oxygen, leading to the loss of carbon dioxide and the production of a variety of byproducts. In the medical field, RuBisCO has been studied as a potential target for the development of new drugs to treat a variety of conditions, including cancer, diabetes, and obesity. Some researchers have also explored the use of RuBisCO as a biosensor for detecting carbon dioxide levels in the environment or as a tool for producing biofuels.
In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.
In the medical field, a protein subunit refers to a smaller, functional unit of a larger protein complex. Proteins are made up of chains of amino acids, and these chains can fold into complex three-dimensional structures that perform a wide range of functions in the body. Protein subunits are often formed when two or more protein chains come together to form a larger complex. These subunits can be identical or different, and they can interact with each other in various ways to perform specific functions. For example, the protein hemoglobin, which carries oxygen in red blood cells, is made up of four subunits: two alpha chains and two beta chains. Each of these subunits has a specific structure and function, and they work together to form a functional hemoglobin molecule. In the medical field, understanding the structure and function of protein subunits is important for developing treatments for a wide range of diseases and conditions, including cancer, neurological disorders, and infectious diseases.
HSP70 heat shock proteins are a family of proteins that are produced in response to cellular stress, such as heat, toxins, or infection. They are also known as heat shock proteins because they are upregulated in cells exposed to high temperatures. HSP70 proteins play a crucial role in the folding and refolding of other proteins in the cell. They act as molecular chaperones, helping to stabilize and fold newly synthesized proteins, as well as assisting in the refolding of misfolded proteins. This is important because misfolded proteins can aggregate and form toxic structures that can damage cells and contribute to the development of diseases such as Alzheimer's, Parkinson's, and Huntington's. In addition to their role in protein folding, HSP70 proteins also play a role in the immune response. They can be recognized by the immune system as foreign antigens and can stimulate an immune response, leading to the production of antibodies and the activation of immune cells. Overall, HSP70 heat shock proteins are important for maintaining cellular homeostasis and protecting cells from damage. They are also of interest in the development of new therapies for a variety of diseases.
Adenosine diphosphate (ADP) is a molecule that plays a crucial role in various metabolic processes in the body, particularly in the regulation of energy metabolism. It is a nucleotide that is composed of adenine, ribose, and two phosphate groups. In the medical field, ADP is often used as a diagnostic tool to assess the function of platelets, which are blood cells that play a critical role in blood clotting. ADP is a potent activator of platelets, and a decrease in platelet aggregation in response to ADP is often an indication of a bleeding disorder. ADP is also used in the treatment of various medical conditions, including heart disease, stroke, and migraines. For example, drugs that inhibit ADP receptors on platelets, such as clopidogrel and ticagrelor, are commonly used to prevent blood clots in patients with heart disease or stroke. Overall, ADP is a critical molecule in the regulation of energy metabolism and the function of platelets, and its role in the medical field is significant.
Urea is a chemical compound that is produced in the liver as a waste product of protein metabolism. It is then transported to the kidneys, where it is filtered out of the blood and excreted in the urine. In the medical field, urea is often used as a diagnostic tool to measure kidney function. High levels of urea in the blood can be a sign of kidney disease or other medical conditions, while low levels may indicate malnutrition or other problems. Urea is also used as a source of nitrogen in fertilizers and as a raw material in the production of plastics and other chemicals.
Chloroplasts are organelles found in plant cells that are responsible for photosynthesis, the process by which plants convert light energy into chemical energy in the form of glucose. Chloroplasts contain chlorophyll, a green pigment that absorbs light energy, and use this energy to power the chemical reactions of photosynthesis. Chloroplasts are also responsible for producing oxygen as a byproduct of photosynthesis. In the medical field, chloroplasts are not typically studied or treated directly, but understanding the process of photosynthesis and the role of chloroplasts in this process is important for understanding plant biology and the role of plants in the environment.
Escherichia coli (E. coli) is a type of bacteria that is commonly found in the human gut. E. coli proteins are proteins that are produced by E. coli bacteria. These proteins can have a variety of functions, including helping the bacteria to survive and thrive in the gut, as well as potentially causing illness in humans. In the medical field, E. coli proteins are often studied as potential targets for the development of new treatments for bacterial infections. For example, some E. coli proteins are involved in the bacteria's ability to produce toxins that can cause illness in humans, and researchers are working to develop drugs that can block the activity of these proteins in order to prevent or treat E. coli infections. E. coli proteins are also used in research to study the biology of the bacteria and to understand how it interacts with the human body. For example, researchers may use E. coli proteins as markers to track the growth and spread of the bacteria in the gut, or they may use them to study the mechanisms by which the bacteria causes illness. Overall, E. coli proteins are an important area of study in the medical field, as they can provide valuable insights into the biology of this important bacterium and may have potential applications in the treatment of bacterial infections.
Cloning, molecular, in the medical field refers to the process of creating identical copies of a specific DNA sequence or gene. This is achieved through a technique called polymerase chain reaction (PCR), which amplifies a specific DNA sequence to produce multiple copies of it. Molecular cloning is commonly used in medical research to study the function of specific genes, to create genetically modified organisms for therapeutic purposes, and to develop new drugs and treatments. It is also used in forensic science to identify individuals based on their DNA. In the context of human cloning, molecular cloning is used to create identical copies of a specific gene or DNA sequence from one individual and insert it into the genome of another individual. This technique has been used to create transgenic animals, but human cloning is currently illegal in many countries due to ethical concerns.
Proteins are complex biomolecules made up of amino acids that play a crucial role in many biological processes in the human body. In the medical field, proteins are studied extensively as they are involved in a wide range of functions, including: 1. Enzymes: Proteins that catalyze chemical reactions in the body, such as digestion, metabolism, and energy production. 2. Hormones: Proteins that regulate various bodily functions, such as growth, development, and reproduction. 3. Antibodies: Proteins that help the immune system recognize and neutralize foreign substances, such as viruses and bacteria. 4. Transport proteins: Proteins that facilitate the movement of molecules across cell membranes, such as oxygen and nutrients. 5. Structural proteins: Proteins that provide support and shape to cells and tissues, such as collagen and elastin. Protein abnormalities can lead to various medical conditions, such as genetic disorders, autoimmune diseases, and cancer. Therefore, understanding the structure and function of proteins is essential for developing effective treatments and therapies for these conditions.
Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.
Cytosol is the fluid inside the cytoplasm of a cell, which is the gel-like substance that fills the cell membrane. It is also known as the cytoplasmic matrix or cytosolic matrix. The cytosol is a complex mixture of water, ions, organic molecules, and various enzymes and other proteins that play important roles in cellular metabolism, signaling, and transport. It is the site of many cellular processes, including protein synthesis, energy production, and waste removal. The cytosol is also the site of many cellular organelles, such as the mitochondria, ribosomes, and endoplasmic reticulum, which are responsible for carrying out specific cellular functions.
Non-chaperonin molecular chaperone ATPase
R. John Ellis
Single particle analysis
Evolution of molecular chaperones
Heat shock response
No data available that match "chaperonins"
- TRiC, the eukaryotic chaperonin, is composed of two rings of eight different though related subunits, each thought to be represented once per eight-membered ring. (wikipedia.org)
- The actin amino acid chain (center) gets folded into the mature 3D-structure inside the cavity of the chaperonin TRiC. (mpg.de)
- Unlike all previously studied proteins, actin cannot acquire its fold in absence of the chaperonin TRiC. (mpg.de)
- The co-evolution of TRiC and actin has allowed actin to "out-source" the responsibility for protein folding to the chaperonin. (mpg.de)
- Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC. (bvsalud.org)
- The hetero-oligomeric chaperonin of eukarya , TRiC, is required to fold the cytoskeletal protein actin . (bvsalud.org)
- ATP binding to TRiC effects an asymmetric conformational change in the chaperonin ring. (bvsalud.org)
- These conformational changes allow the chaperonin to bind an unfolded or misfolded protein, encapsulate that protein within one of the cavities formed by the two rings, and release the protein back into solution. (wikipedia.org)
- HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. (wikipedia.org)
- Chaperonin proteins may also tag misfolded proteins to be degraded. (wikipedia.org)
- Chaperonins undergo large conformational changes during a folding reaction as a function of the enzymatic hydrolysis of ATP as well as binding of substrate proteins and cochaperonins, such as GroES. (wikipedia.org)
- The exact mechanism by which chaperonins facilitate folding of substrate proteins is unknown. (wikipedia.org)
- Group II Heat Shock Protein 60 chaperonins which catalyses the cytoplasmic ATP-dependent folding of newly synthesized proteins. (yeastgenome.org)
- The structure of this protein suggests that it may act as a chaperonin, which is a protein that helps fold other proteins. (medlineplus.gov)
- For the sensitivity of the three Anti·His Antibodies in detecting this panel of proteins see the figure Sensitivity of anti·His antibodies. Detection of 6xHis-tagged proteins with Anti·His Antibodies (Tetra·His Antibody in the center). A: DHFR; B: DHFR; C: thioredoxin; D: TNF-α; E: TFIIA γ ; F: chaperonin; G DNA polymerase; H: TFIIAαß; for tag location and sequences detected see table 'Proteins detected with QIA express Anti·His Antibodies'. Indicated amounts of pure 6xHis-tagged protein were applied to a nitrocellulose membrane, and detection was carried out with the Anti·His primary antibody indicated diluted 1/2000, followed by chromogenic detection with AP-conjugated rabbit anti-mouse IgG and NBT/BCIP. "> "Sensitivity of QIA express Anti·His Antibodies" ). (qiagen.com)
- Group I chaperonins (Cpn60) are found in bacteria as well as organelles of endosymbiotic origin: chloroplasts and mitochondria. (wikipedia.org)
- The GroEL/GroES complex in E. coli is a Group I chaperonin and the best characterized large (~ 1 MDa) chaperonin complex. (wikipedia.org)
- Conformational changes in the chaperonin GroEL: New insights into the allosteric mechanism. (mpg.de)
- The simpler bacterial chaperonin system, GroEL/GroES, is unable to mediate actin folding. (bvsalud.org)
- Group II chaperonins are not thought to utilize a GroES-type cofactor to fold their substrates. (wikipedia.org)
- Unfolding the role of chaperones and chaperonins in human disease. (medlineplus.gov)
- Some bacteria use multiple copies of this chaperonin, probably for different peptides. (wikipedia.org)
- This step induces the partial release of actin , priming it for folding upon complete release into the chaperonin cavity, mediated by ATP hydrolysis . (bvsalud.org)
- 2001). Expression of the chaperonin 10 gene during zebrafish development . (sgu.edu)
- The structure of these chaperonins resemble two donuts stacked on top of one another to create a barrel. (wikipedia.org)
- Although the structure of the MKKS protein is similar to that of a chaperonin, some studies have suggested that protein folding may not be this protein's primary function. (medlineplus.gov)
- There is a newsgroup-type interface available on the Chaperonin Web Page that allows you to post and read messages just like usenet. (bio.net)
- Each ring is composed of either 7, 8 or 9 subunits depending on the organism in which the chaperonin is found. (wikipedia.org)
- In this article, we describe the structure and function of chaperones in bacterial and eukaryotic cells, focusing on the chaperonin class of chaperones. (nih.gov)
- Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes. (nih.gov)
- We suggest that transient ring separation is an integral part of the chaperonin mechanism. (bvsalud.org)
- 14. 60KDa chaperonin (HSP60) is over-expressed during colorectal carcinogenesis. (nih.gov)
- In the absence of the eukaryotic type II chaperonin complex, CCT, T cell activation induced changes in the proteome are compromised including the formation of nuclear actin filaments and the formation of a normal cell stress response. (ox.ac.uk)
- Upon release, the substrate protein will either be folded or will require further rounds of folding, in which case it can again be bound by a chaperonin. (wikipedia.org)
- Clare, Daniel K. and Vasishtan, Daven and Stagg, S. and Quispe, J. and Farr, G.W. and Topf, Maya and Horwich, A.L. and Saibil, Helen R. (2012) ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL Chaperonin. (bbk.ac.uk)
- The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actions of binding and encapsulation. (bbk.ac.uk)
- GroEL Ring Separation and Exchange in the Chaperonin Reaction. (bvsalud.org)
- 80 °C)] synthesize intrinsically thermostable cellular components and/or extrinsic stabilizing factors (chaperonins and polyamines, for example). (asmblog.org)
- A homo-16mer in some archaea, it is regarded as the prototypical type II chaperonin. (wikipedia.org)
- It might represent another ancient type of chaperonin. (wikipedia.org)
- There is a newsgroup-type interface available on the Chaperonin Web Page that allows you to post and read messages just like usenet. (bio.net)
- The family of chaperonins is split into GROUP I CHAPERONINS , and GROUP II CHAPERONINS , with each group having its own repertoire of protein subunits and subcellular preferences. (nih.gov)