A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. 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.
A subcategory of chaperonins found in ARCHAEA and the CYTOSOL of eukaryotic cells. Group II chaperonins form a barrel-shaped macromolecular structure that is distinct from GROUP I CHAPERONINS in that it does not utilize a separate lid like structure to enclose proteins.
A group I chaperonin protein that forms a lid-like structure which encloses the non-polar cavity of the chaperonin complex. The protein was originally studied in BACTERIA where it is commonly referred to as GroES protein.
A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.
A subcategory of chaperonins found in MITOCHONDRIA; CHLOROPLASTS; and BACTERIA. Group I chaperonins form into a barrel-shaped macromolecular structure that is enclosed by a separate lid-like protein component.
A group II chaperonin found in eukaryotic CYTOSOL. It is comprised of eight subunits with each subunit encoded by a separate gene. This chaperonin is named after one of its subunits which is a T-COMPLEX REGION-encoded polypeptide.
Group II chaperonins found in species of ARCHAEA.
An enzyme that catalyzes the transfer of the planetary sulfur atom of thiosulfate ion to cyanide ion to form thiocyanate ion. EC
A 20 cM region of mouse chromosome 17 that is represented by a least two HAPLOTYPES. One of the haplotypes is referred to as the t-haplotype and contains an unusual array of mutations that affect embryonic development and male fertility. The t-haplotype is maintained in the gene pool by the presence of unusual features that prevent its recombination.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
A genus of extremely thermophilic heterotrophic archaea, in the family THERMOCOCCACEAE, occurring in heated sea flows. They are anaerobic chemoorganotropic sulfidogens.
Conformational transitions of a protein from unfolded states to a more folded state.
Proteins found in any species of archaeon.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC
Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.
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.
Cells of the higher organisms, containing a true nucleus bounded by a nuclear membrane.
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
Cells lacking a nuclear membrane so that the nuclear material is either scattered in the cytoplasm or collected in a nucleoid region.
Proteins found in any species of bacterium.
A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. It can also utilize OXYGEN as a substrate to catalyze the synthesis of 2-phosphoglycolate and 3-phosphoglycerate in a process referred to as photorespiration.
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).
A genus of anaerobic coccoid METHANOCOCCACEAE whose organisms are motile by means of polar tufts of flagella. These methanogens are found in salt marshes, marine and estuarine sediments, and the intestinal tract of animals.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
A genus of aerobic, chemolithotrophic, coccoid ARCHAEA whose organisms are thermoacidophilic. Its cells are highly irregular in shape, often lobed, but occasionally spherical. It has worldwide distribution with organisms isolated from hot acidic soils and water. Sulfur is used as an energy source.
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.
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.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The process of cleaving a chemical compound by the addition of a molecule of water.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
The diversion of RADIATION (thermal, electromagnetic, or nuclear) from its original path as a result of interactions or collisions with atoms, molecules, or larger particles in the atmosphere or other media. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.
The rate dynamics in chemical or physical systems.
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.
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.
Proteins obtained from ESCHERICHIA COLI.
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.
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.
Proteins prepared by recombinant DNA technology.
Processes occurring in various organisms by which new genes are copied. Gene duplication may result in a MULTIGENE FAMILY; supergenes or PSEUDOGENES.
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.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
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.

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.

The original chaperonin is proposed to have evolved from a peroxiredoxin. Group I chaperonins (Cpn60) are found in bacteria as ... In archaea, the chaperonin is called the thermosome. In eukarya, the cytoplasmic chaperonin is called CCT (also called TRiC). ... The active chaperonin role is in turn involved with specific chaperonin-substrate interactions that may be coupled to ... The GroEL/GroES complex in E. coli is a Group I chaperonin and the best characterized large (~ 1 MDa) chaperonin complex. GroEL ...
1996). The Chaperonins. San Diego: Academic Press. pp. -. Ranson NA, White HE, Saibil HR (July 1998). "Chaperonins". The ... Chaperonin ATPase (EC, chaperonin) is an enzyme with systematic name ATP phosphohydrolase (polypeptide-unfolding). This ... Chaperonin Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ (May 1988). " ... Chaperonin+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (CS1: long volume ...
... (EC, molecular chaperone Hsc70 ATPase) is an enzyme with systematic name ATP ... Non-chaperonin+molecular+chaperone+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: ... phosphate These enzymes perform many functions that are similar to those of chaperonins. Chaperone (protein) Sadis S, Hightower ...
Biological machines Chaperome Chaperonin Chemical chaperones Heat shock protein Heat shock factor 1 Molecular chaperone therapy ... The Hsp60 family of protein chaperones are termed chaperonins, and are characterized by a stacked double-ring structure and are ... Fenton WA, Horwich AL (May 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Quarterly Reviews of ... Martin J, Hartl FU (February 1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proceedings ...
Group 2 chaperonins are found in the cytosol of eukaryotic cells as well as in archaea. Group 2 chaperonins also contain an ... Chaperonins are divided into two groups. Group 1 chaperonins are commonly found in bacteria, chloroplasts, and mitochondria. ... All chaperonins exhibit two states (open and closed), between which they can cycle. This cycling process is important during ... Chaperonins are a special class of chaperones that promote native state folding by cyclically encapsulating the peptide chain. ...
1988: Discovery of the chaperonins. 2000: First demonstration that macromolecular crowding affects protein folding and ... "pioneering research on the chaperonins". 2011: Croonian Prize Lecture of the Royal Society for "pioneering contributions to ...
Binding of GroES to the open cavity of the chaperonin induces the individual subunits of the chaperonin to rotate such that the ... Alternate Names: 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, HuCHA60, Mitochondrial matrix protein ... this is not the case with chaperonins". It has been found that many anti-chaperonin antibodies exist and are associated with ... "generated by a human host after exposure to bacterial chaperonin 60 proteins" can cross-react with human chaperonin 60 proteins ...
This group II chaperonin is an ATP-dependent chaperonin that is responsible for folding or refolding of incipient or denatured ... Being a Group II chaperonin, the thermosome has a similar structure to group I chaperonins. The main difference, however, lies ... A thermosome is a group II chaperonin protein complex that functions in archaea. It is the homolog of eukaryotic CCT. ... Similar to the GroEL chaperonins in bacteria, the thermosome shows negative cooperativity since the two rings of the thermosome ...
Trent JD, Kagawa HK, Yaoi T, Olle E, Zaluzec NJ (May 1997). "Chaperonin filaments: the archaeal cytoskeleton?". Proceedings of ...
... bonds specifically to cytosolic chaperonin protein. This complex of prefoldin and chaperonin then forms molecules of ... due to its high affinity for the chaperonin molecule. Once the prefoldin is in contact with the chaperonin protein, it loses ... For example, the prefoldin that is used in the formation of actin also transfers α or β tubulin to a cytosolic chaperonin. The ... A prefoldin molecule works as a transfer protein in conjunction with a molecule of chaperonin to form a chaperone complex and ...
"Entrez Gene: TBCE tubulin folding cofactor E". Lewis SA, Tian G, Vainberg IE, Cowan NJ (1996). "Chaperonin-mediated folding of ... Roobol A, Sahyoun ZP, Carden MJ (1999). "Selected subunits of the cytosolic chaperonin associate with microtubules assembled in ...
Lewis SA, Tian G, Vainberg IE, Cowan NJ (1996). "Chaperonin-mediated folding of actin and tubulin". J. Cell Biol. 132 (1-2): 1- ...
This gene encodes chaperonin cofactor A. GRCh38: Ensembl release 89: ENSG00000171530 - Ensembl, May 2017 GRCm38: Ensembl ... "Entrez Gene: TBCA tubulin folding cofactor A". Lewis SA, Tian G, Vainberg IE, Cowan NJ (1996). "Chaperonin-mediated folding of ...
These hexameric HSP100/Clp proteins produce ring like structures resembling chaperonins. The Clp proteases have a two-component ...
"Symmetric Complexes of GroE Chaperonins as Part of the Functional Cycle". Science. American Association for the Advancement of ...
Methanococcus maripaludis chaperonin, reconstructed to 0.43 nanometer resolution. This bacterial protein complex is a machine ... January 2010). "Mechanism of folding chamber closure in a group II chaperonin". Nature. 463 (7279): 379-83. Bibcode:2010Natur. ...
The homolog in E. coli is GroES that is a chaperonin which usually works in conjunction with GroEL. GroES exists as a ring- ... Heat shock 10 kDa protein 1 (Hsp10), also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF), is a protein that in ... "Entrez Gene: HSPE1 heat shock 10kDa protein 1 (chaperonin 10)". Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT ... Lee KH, Kim HS, Jeong HS, Lee YS (October 2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial ...
Foldase Chaperonin Co-chaperone Hoffmann, J. R. H.; Linke, K.; Graf, P. C.; Lilie, H.; Jakob, U. (2003). "Identification of a ...
doi:10.1046/j.1461-0248.2003.00528.x. Williams TA, Fares MA (21 July 2010). "The effect of chaperonin buffering on protein ... Gupta RS (January 1995). "Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of ... Phylogenetic analysis using two families of HSPs (hsp10 and hsp60, also called chaperonins) support the current endosymbiosis ...
Nobuhiko Tokuriki; Dan S. Tawfik (2009). "Chaperonin overexpression promotes genetic variation and enzyme evolution". Nature. ...
"Knot formation in newly translated proteins is spontaneous and accelerated by chaperonins". Nat Chem Biol. 8 (2): 147-153. doi: ... "The exclusive effects of chaperonin on the behavior of proteins with 52 knot". PLOS Computational Biology. 14 (3): e1005970. ...
"Entrez Gene: CCT3 chaperonin containing TCP1, subunit 3 (gamma)". Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault ... which encodes the chaperonin subunit CCT gamma". The Biochemical Journal. 313 (Pt 2): 381-9. doi:10.1042/bj3130381. PMC 1216920 ... "Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC". Molecular Cell. 4 (6): 1051-61. ... "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Current Biology. 4 ( ...
"Entrez Gene: CCT8 chaperonin containing TCP1, subunit 8 (theta)". Human CCT8 genome location and CCT8 gene details page in the ... Kubota H, Hynes G, Willison K (Apr 1995). "The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin ... Yokota S, Yanagi H, Yura T, Kubota H (2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a ... TCP1, T-complex protein 1 subunit alpha Chaperonin GRCh38: Ensembl release 89: ENSG00000156261 - Ensembl, May 2017 GRCm38: ...
"Entrez Gene: CCT7 chaperonin containing TCP1, subunit 7 (eta)". Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M ... Hynes G, Celis JE, Lewis VA, Carne A, U S, Lauridsen JB, Willison KR (Nov 1996). "Analysis of chaperonin-containing TCP-1 ... Yokota S, Yanagi H, Yura T, Kubota H (Sep 2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content ... chaperonin containing TCP1) from the subunit composition of CCT micro-complexes". The EMBO Journal. 16 (14): 4311-6. doi: ...
"Entrez Gene: CCT4 chaperonin containing TCP1, subunit 4 (delta)". Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault ... Melki R, Batelier G, Soulié S, Williams RC (May 1997). "Cytoplasmic chaperonin containing TCP-1: structural and functional ... "Eukaryotic type II chaperonin CCT interacts with actin through specific subunits". Nature. 402 (6762): 693-6. Bibcode:1999Natur ... "Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin". Journal of Structural ...
CCT is a group II chaperonin, a large protein complex that assists in the folding of other proteins. CCT is formed of a double ... After AMP-PNP is bound to CCT the substrates move within the chaperonin's cavity. It also seems that in the case of actin, the ... The actin is recognized, loaded, and delivered to the cytosolic chaperonin (CCT) in an open conformation by the inner end of ... Brackley KI, Grantham J (Jan 2009). "Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle ...
"Entrez Gene: CCT5 chaperonin containing TCP1, subunit 5 (epsilon)". Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, ... Yokota S, Yanagi H, Yura T, Kubota H (Sep 2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content ... Roobol A, Holmes FE, Hayes NV, Baines AJ, Carden MJ (Apr 1995). "Cytoplasmic chaperonin complexes enter neurites developing in ... Liou AK, Willison KR (Jul 1997). "Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit ...
"Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)". Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault ... Yokota S, Yanagi H, Yura T, Kubota H (Sep 2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content ... Hynes GM, Willison KR (Jun 2000). "Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding ... "3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin". Nature ...
Once a cap binds to the chaperonin, the protein is free within the barrel to undergo hydrophobic collapse and reach a stable ... Chaperones include the HSP70s and HSP90s while HSP60s are considered to be chaperonins. The HSP70 chaperone family is the main ... Todd MJ, Lorimer GH, Thirumalai D (April 1996). "Chaperonin-facilitated protein folding: optimization of rate and yield by an ... Kmiecik S, Kolinski A (July 2011). "Simulation of chaperonin effect on protein folding: a shift from nucleation-condensation to ...
"Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles". Nature. 423 (6940): 628-632. ... ATP-responsive nanotubular carriers composed of chaperonin proteins, a biomolecular machine (4) non-crosslinked photoactuators ...

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)
  • Group II chaperonins (TCP-1), found in the eukaryotic cytosol and in archaea, are more poorly characterized. (wikipedia.org)
  • The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins. (yeastgenome.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)
  • This gene encodes a member of the chaperonin family. (thermofisher.com)
  • 2002). Expression and genomic organization of the zebrafish chaperonin gene complex . (sgu.edu)
  • Greek students were pathogen: specific identification by the chaperonin 60 gene identification method. (cdc.gov)
  • A homo-16mer in some archaea, it is regarded as the prototypical type II chaperonin. (wikipedia.org)
  • The thermosome (Ths) chaperonin family represents the most salient PHX genes among Archaea. (wikigenes.org)
  • 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)