Chaperonin Containing TCP-1: 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.Chaperonin 10: 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.Chaperonin 60: 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.Chaperonins: 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.Group II Chaperonins: 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.t-Complex Genome Region: 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.Thiosulfate Sulfurtransferase: An enzyme that catalyzes the transfer of the planetary sulfur atom of thiosulfate ion to cyanide ion to form thiocyanate ion. EC 2.8.1.1.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Thermosomes: Group II chaperonins found in species of ARCHAEA.Group I Chaperonins: 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.Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Gram-Positive Asporogenous Rods, Irregular: A group of irregular rod-shaped bacteria that stain gram-positive and do not produce endospores.Adenosine Triphosphate: 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.Archaeal Proteins: Proteins found in any species of archaeon.Protein Refolding: Conformational transitions of a protein from unfolded states to a more folded state.Heat-Shock Proteins: 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.Molecular Chaperones: 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.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Ribulose-Bisphosphate Carboxylase: 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.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Methanococcus: 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.Thermococcus: A genus of extremely thermophilic heterotrophic archaea, in the family THERMOCOCCACEAE, occurring in heated sea flows. They are anaerobic chemoorganotropic sulfidogens.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Protein Denaturation: Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.Sulfolobus: 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.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Adenosine Triphosphatases: 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.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Protein Subunits: 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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Cryoelectron Microscopy: Electron microscopy involving rapid freezing of the samples. The imaging of frozen-hydrated molecules and organelles permits the best possible resolution closest to the living state, free of chemical fixatives or stains.Bacterial Proteins: Proteins found in any species of bacterium.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Eukaryotic Cells: Cells of the higher organisms, containing a true nucleus bounded by a nuclear membrane.Adenylyl Imidodiphosphate: 5'-Adenylic acid, monoanhydride with imidodiphosphoric acid. An analog of ATP, in which the oxygen atom bridging the beta to the gamma phosphate is replaced by a nitrogen atom. It is a potent competitive inhibitor of soluble and membrane-bound mitochondrial ATPase and also inhibits ATP-dependent reactions of oxidative phosphorylation.Hot Temperature: Presence of warmth or heat or a temperature notably higher than an accustomed norm.Adenosine Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Alcohol Dehydrogenase: A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.3-Isopropylmalate Dehydrogenase: An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.Tubulin: A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from SPERM FLAGELLUM; CILIA; and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to COLCHICINE; VINCRISTINE; and VINBLASTINE.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Archaea: 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.Thermus thermophilus: A species of gram-negative, aerobic, rod-shaped bacteria found in hot springs of neutral to alkaline pH, as well as in hot-water heaters.Kinetics: The rate dynamics in chemical or physical systems.Protein Renaturation: The reconstitution of a protein's activity following denaturation.Aeropyrum: A genus of anaerobic, chemolithotropic coccoid ARCHAEA, in the family DESULFUROCOCCACEAE. They live in marine environments.Citrate (si)-Synthase: Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Substrate Cycling: A set of opposing, nonequilibrium reactions catalyzed by different enzymes which act simultaneously, with at least one of the reactions driven by ATP hydrolysis. The results of the cycle are that ATP energy is depleted, heat is produced and no net substrate-to-product conversion is achieved. Examples of substrate cycling are cycling of gluconeogenesis and glycolysis pathways and cycling of the triglycerides and fatty acid pathways. Rates of substrate cycling may be increased many-fold in association with hypermetabolic states resulting from severe burns, cold exposure, hyperthyroidism, or acute exercise.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Methanobacterium: A genus of anaerobic, rod-shaped METHANOBACTERIACEAE. Its organisms are nonmotile and use ammonia as the sole source of nitrogen. These methanogens are found in aquatic sediments, soil, sewage, and the gastrointestinal tract of animals.Multiprotein Complexes: Macromolecular complexes formed from the association of defined protein subunits.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Anilino Naphthalenesulfonates: A class of organic compounds which contain an anilino (phenylamino) group linked to a salt or ester of naphthalenesulfonic acid. They are frequently used as fluorescent dyes and sulfhydryl reagents.Guanidine: A strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant. (From Martindale, the Extra Pharmacopoeia, 30th ed and Merck Index, 12th ed) It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC.Urea: 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.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Microtubule-Associated Proteins: High molecular weight proteins found in the MICROTUBULES of the cytoskeletal system. Under certain conditions they are required for TUBULIN assembly into the microtubules and stabilize the assembled microtubules.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Actins: Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Thermoplasma: A genus of facultatively anaerobic heterotrophic archaea, in the order THERMOPLASMALES, isolated from self-heating coal refuse piles and acid hot springs. They are thermophilic and can grow both with and without sulfur.Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Mitochondria: 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)HSP70 Heat-Shock Proteins: 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.Microscopy, Electron: Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.Isocitrate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Spectrometry, Fluorescence: Measurement of the intensity and quality of fluorescence.Tetrahydrofolate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.Allosteric Regulation: The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Chloroplasts: 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.Desulfurococcaceae: A family of archaea, in the order DESULFUROCOCCALES, consisting of anaerobic cocci which utilize peptides, proteins or carbohydrates facultatively by sulfur respiration or fermentation. There are eight genera: AEROPYRUM, Desulfurococcus, Ignicoccus, Staphylothermus, Stetteria, Sulfophoboccus, Thermodiscus, and Thermosphaera. (From Bergey's Manual of Systematic Bacteriology, 2d ed)Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.

Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages. (1/1959)

Both chlamydial and human heat shock protein 60s (HSP 60), which colocalize in human atheroma, may contribute to inflammation during atherogenesis. We tested the hypothesis that chlamydial or human HSP 60 activates human endothelial cells (ECs), smooth muscle cells (SMCs), and monocyte-derived macrophages. We examined the expression of adhesion molecules such as endothelial-leukocyte adhesion molecule-1 (E-selectin), intercellular adhesion molecule-1 (ICAM-1), and vascular cell adhesion molecule-1 (VCAM-1), and the production of the proinflammatory cytokine interleukin-6 (IL-6). We also tested whether either HSP 60 induces nuclear factor-kappaB (NF-kappaB), which contributes to the gene expression of these molecules. Either chlamydial or human HSP 60 induced E-selectin, ICAM-1, and VCAM-1 expression on ECs similar to levels induced by Escherichia coli lipopolysaccharide (LPS). Each HSP 60 also significantly induced IL-6 production by ECs, SMCs, and macrophages to an extent similar to that induced by E. coli LPS, as assessed by enzyme-linked immunosorbent assay (ELISA). In ECs, either HSP 60 triggered activation of NF-kappaB complexes containing p65 and p50 Rel proteins. Heat treatment abolished all these effects, but did not alter the ability of E. coli LPS to induce these functions. Chlamydial and human HSP 60s therefore activate human vascular cell functions relevant to atherogenesis and lesional complications. These findings help to elucidate the mechanisms by which a chronic asymptomatic chlamydial infection might contribute to the pathophysiology of atheroma.  (+info)

Hsp60 is targeted to a cryptic mitochondrion-derived organelle ("crypton") in the microaerophilic protozoan parasite Entamoeba histolytica. (2/1959)

Entamoeba histolytica is a microaerophilic protozoan parasite in which neither mitochondria nor mitochondrion-derived organelles have been previously observed. Recently, a segment of an E. histolytica gene was identified that encoded a protein similar to the mitochondrial 60-kDa heat shock protein (Hsp60 or chaperonin 60), which refolds nuclear-encoded proteins after passage through organellar membranes. The possible function and localization of the amebic Hsp60 were explored here. Like Hsp60 of mitochondria, amebic Hsp60 RNA and protein were both strongly induced by incubating parasites at 42 degreesC. 5' and 3' rapid amplifications of cDNA ends were used to obtain the entire E. histolytica hsp60 coding region, which predicted a 536-amino-acid Hsp60. The E. histolytica hsp60 gene protected from heat shock Escherichia coli groEL mutants, demonstrating the chaperonin function of the amebic Hsp60. The E. histolytica Hsp60, which lacked characteristic carboxy-terminal Gly-Met repeats, had a 21-amino-acid amino-terminal, organelle-targeting presequence that was cleaved in vivo. This presequence was necessary to target Hsp60 to one (and occasionally two or three) short, cylindrical organelle(s). In contrast, amebic alcohol dehydrogenase 1 and ferredoxin, which are bacteria-like enzymes, were diffusely distributed throughout the cytosol. We suggest that the Hsp60-associated, mitochondrion-derived organelle identified here be named "crypton," as its structure was previously hidden and its function is still cryptic.  (+info)

Effect of transforming growth factor beta on experimental Salmonella typhimurium infection in mice. (3/1959)

We have investigated the effect of the in vivo administration of recombinant transforming growth factor beta (rTGF-beta) on the pathogenic mechanisms involved in Salmonella typhimurium experimental infection in mice. The protective response elicited by macrophages was induced by rTGF-beta1 by 2 days after experimental infection, as demonstrated by an increased NO production, while the humoral protective effect began with cytokine mRNA expression 2 days after the challenge and continued after 5 days with cytokine release and lymphocyte activation. We demonstrated that all mice who received rTGF-beta1 survived 7 days after infection. The number of bacteria recovered in the spleens and in the livers of rTGF-beta1-treated mice 2 and 5 days after infection was significantly smaller than that found in the same organs after phosphate-buffered saline (PBS) inoculation. Furthermore, 2 and 5 days after infection, splenic macrophages from rTGF-beta1-treated mice showed a greater NO production than did those from PBS-treated mice. The effect of rTGF-beta1 on S. typhimurium infection in mice was correlated with the expression of cell costimulatory CD28 molecules. Five days after S. typhimurium infection, the percentage of CD28(+)-expressing T cells in splenic lymphocytes from rTGF-beta1-treated mice increased with respect to that from control mice. Gamma interferon (IFN-gamma) mRNA was present in a greater amount in spleen cells from rTGF-beta1-treated mice after 2 days, although the intensity of the band decreased 5 days after the challenge. A similar pattern was obtained with the mRNAs for interleukin-1alpha (IL-1alpha), IL-6, TGF-beta, and inducible nitric oxide synthase, which showed greater expression in cells obtained from rTGF-beta1-treated and S. typhimurium-infected mice 2 days after challenge. The treatment with rTGF-beta1 induced an increase in IL-1alpha and IFN-gamma release in the supernatant of splenocyte cultures 5 days after the experimental infection with S. typhimurium. Moreover, we demonstrated that 5 days after infection, the IFN-gamma titer was significantly greater in the sera of rTGF-beta-treated mice than in those of PBS-treated mice. Also, hsp60 showed greater expression 2 days after the challenge in splenocytes from rTGF-beta1-treated mice. The role played by proinflammatory and immunoregulatory cytokines and by CD28 is discussed.  (+info)

Conformational changes generated in GroEL during ATP hydrolysis as seen by time-resolved infrared spectroscopy. (4/1959)

Changes in the vibrational spectrum of the chaperonin GroEL in the presence of ADP and ATP have been followed as a function of time using rapid scan Fourier transform infrared spectroscopy. The interaction of nucleotides with GroEL was triggered by the photochemical release of the ligands from their corresponding biologically inactive precursors (caged nucleotides; P3-1-(2-nitro)phenylethyl nucleotide). Binding of either ADP or ATP induced the appearance of small differential signals in the amide I band of the protein, sensitive to protein secondary structure, suggesting a subtle and localized change in protein conformation. Moreover, conformational changes associated with ATP hydrolysis were detected that differed markedly from those observed upon nucleotide binding. Both, high-amplitude absorbance changes and difference bands attributable to modifications in the interaction between oppositely charged residues were observed during ATP hydrolysis. Once this process had occurred, the protein relaxed to an ADP-like conformation. Our results suggest that the secondary structure as well as salt bridges of GroEL are modified during ATP hydrolysis, as compared with the ATP and ADP bound protein states.  (+info)

Enhanced fatty streak formation in C57BL/6J mice by immunization with heat shock protein-65. (5/1959)

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)

Physiological states of individual Salmonella typhimurium cells monitored by in situ reverse transcription-PCR. (6/1959)

The possibility of using levels of specific mRNAs in individual bacteria as indicators of single-cell physiology was investigated. Estimates of the numbers of groEL and tsf mRNAs per cell in Salmonella typhimurium cells in different physiological states were obtained by Northern analysis. The average number of groEL mRNAs per cell was estimated to be 22 in fast-growing cultures and 197 in heat-shocked cultures. The average number of tsf mRNAs per cell was estimated to be 37 in fast-growing cultures, 4 in slow-growing cultures, and 0 in nongrowing cultures. The potential of mRNA-targeted in situ reverse transcription (RT)-PCR to monitor quantitatively different levels of groEL and tsf mRNA in individual cells and thus monitor both specific gene induction and general growth activity was assessed. Neither groEL nor tsf mRNA was present in stationary-phase cells, but it was shown that stationary-phase cells contain other RNA species at high levels, which may provide a possibility for monitoring directly stationary-phase individual cells by the use of in situ RT-PCR. The outcome of the in situ RT-PCR analyses indicated that a population of fast-growing cells is heterogeneous with respect to groEL mRNA single-cell contents, suggesting a cell-cycle-controlled expression of groEL in S. typhimurium, whereas a fast-growing culture is homogeneous with respect to tsf mRNA single-cell contents, suggesting that the level of tsf mRNA is relatively constant during the cell cycle.  (+info)

Molecular chaperones: pathways and networks. (7/1959)

Some proteins synthesized by growing eukaryotic cells are transferred along unidirectional pathways of molecular chaperones until the risk of aggregation has decreased and they can be released safely. Mature proteins denatured by stress may instead be handled by chaperones acting in branched, reversible networks.  (+info)

Identification of Mycobacterium kansasii by using a DNA probe (AccuProbe) and molecular techniques. (8/1959)

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)

The human heat-shock protein multigene family comprises several highly conserved proteins with structural and functional properties in common, but which vary in the extent of their inducibility in response to metabolic stress. We have isolated and characterized a novel human HSP70 cDNA, HSP70B cDNA, and its corresponding gene sequence. HSP70B cDNA hybrid-selected an mRNA encoding a more basic 70 kDa heat-shock protein than both the major stress-inducible HSP70 and constitutively expressed HSC70 heat-shock proteins, which in common with other heat-shock 70 kDa proteins bound ATP. The complete HSP70B gene was sequenced and, like the major inducible HSP70 gene, is devoid of introns. The HSP70B gene has 77% sequence similarity to the HSP70 gene and 70% similarity to HSC70 cDNA, with greatest sequence divergence towards the 3-terminus. The HSP70B gene represents a functional gene, as indicated by Northern-blot analysis with specific oligonucleotides, hybrid-selected translation with a specific ...
Aggregatibacter actinomycetemcomitans (Aa) expresses a 64-kDa GroEL protein belonging to the heat shock family of proteins. This protein has been shown to influence human host cells, but the apoptotic capacity of the GroEL protein regarding T cells is not yet known. The purpose of this study was to investigate the ability of A. actinomycetemcomitans GroEL (AaGroEL) protein to induce human peripheral blood T-cell apoptosis. Endogenous, purified AaGroEL protein was used as an antigen. In AaGroEL-treated T cells, the data indicated that phosphatidylserine exposure, an early apoptotic event, was dose- and time-dependent. The AaGroEL-treated T cells were also positive for active caspase-3 in a dose-dependent manner. The rate of AaGroEL-induced apoptosis was suppressed by the addition of the general caspase inhibitor Z-VAD-FMK. Furthermore, cleaved caspase-8 bands (40/36 kDa and 23 kDa) were identified in cells responding to AaGroEL. DNA fragmentation was also detected in the AaGroEL-treated T cells. ...
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Seropositivity to Cp-HSP60 was detected in 217 (99%) of 219 patients with ACS but in only 8 (20%) of 40 patients with SA and in none of the control subjects (P=0.0001, ACS patients versus control subjects; P=0.003, ACS patients versus SA patients; and P=0.05, SA patients versus control subjects). Seropositivity to Cp was detected in 67%, 60%, and 30% of ACS patients, SA patients, and control subjects, respectively (P=0.001, ACS and SA patients versus control subjects). Elevated hs-CRP was found in 60% of ACS patients versus 25% of SA patients and 8% of control subjects (P,0.001, ACS patients versus SA patients and control subjects). Considering the cutoff level of 0.40, Cp-HSP60 IgG antibody levels had 99% specificity and 94% sensitivity for ACS. No differences in anti-Cp-HSP60 or in anti-Cp IgG antibody titers and prevalence of seropositivity were observed between AMI and UA patients (Table) or, in patients with UA, between those with (n=65) and those without (n=114) raised TnT levels. ...
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1SS8: Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
1SS8: Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
Hspe1 (untagged) - Mouse heat shock protein 1 (chaperonin 10) (Hspe1), nuclear gene encoding mitochondrial protein, (10ug), 10 µg.
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GROEL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 572 aa (27-573 a.a.) and having a molecular mass of 60kDa.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
doubles mentioned above are plotted, together with a selected list of 6 small singles particularly deficient in red tissues. They are, 1904 double once in 10, 1902 double once in 10, 1899 single, 1895 single, 1894 single, and 1880 double once in 10. In these it is evident that drought in the spring stops the growth of the tree. The double ring, therefore, seems to be an intermediate form between the large normal single ring, growing through the warm parts of the year, and the small, deficient ring, ending its growth by midsummer. This occasional failure to benefit by the summer rains probably explains why the Prescott trees do not show an agreement of more than about 70 per cent between growth and rainfall. It suggests also that the Flagstaff trees, which grow under conditions of more rainfall and have very few double rings, give a more accurate record than those of Prescott.. Consistent with this view of the doubling is the condition of the outer ring in the Prescott sections collected by Mr. ...
CPn0134 is orthologously related to CT110: residues 1-544 of CPn0134 are 91% similar to residues 1-544 of CT110, a predicted 60 kD chaperonin (protein cpn60, GroEL protein) & (57 kD chlamydial hypersensitivity antigen; HSP60) from C. trachomatis ...
Gribun A, Kimber MS, Ching R, Sprangers R, Fiebig KM & Houry WA (2005) The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J Biol Chem 280, 16185-96. PubMed ...
Mouse Monoclonal Anti-HSP60 Antibody (GROEL/730) [HRP]. Mitochondrial Marker. Validated: WB, ELISA, Flow, ICC/IF, IHC-Fr, IHC-P, IP. Tested Reactivity: Human. 100% Guaranteed.
高い抗原親和性、特異性と安定した品質を兼ね備えたアブカムのウサギ・モノクローナル抗体 RabMAb® ab45133 交差種: Rat,Hu 適用: WB,IHC-P,Flow Cyt,ICC/IF
高い抗原親和性、特異性と安定した品質を兼ね備えたアブカムのウサギ・モノクローナル抗体 RabMAb® ab62339 交差種: Hu 適用: WB,IHC-P,ICC
The human mitochondrial chaperonin is a macromolecular machine that catalyzes the proper folding and assembly of newly imported mitochondrial proteins into their biologically active state. It is composed of two proteins from the highly conserved heat shock protein family, hsp10 and hsp60, that assemble into large oligomeric complexes responsible for mediating the folding of non-native polypeptides in an ATP dependent manner. In addition to its innate role in protein folding, human mitochondrial hsp60 has been implicated in numerous moonlighting cellular activities that have been linked to diseases conditions such as cancer and neurodegeneracy. In light of its cellular importance, the conditions that propel the human mitochondrial chaperonin through its protein folding mechanism are not well understood. Here I propose a protein folding scheme for the mitochondrial chaperonin based on negative stain electron microscopy 3-D reconstructions. I found that the human mitochondrial chaperonin complex
GroEL/GroES is the only chaperone machine of E. coli that is absolutely essential for bacterial survival under all laboratory conditions tested (Fayetet al. 1989). GroEL/GroES homologs are found in all organisms except in some Archaea species (Macarioet al. 1999) and the recently sequenced Ureaplasmum urealyticum mycobacterium (Glasset al. 2000). The E. coli GroEL chaperone can function not only with its own GroES cochaperone, but also with bacteriophage-encoded cochaperones, such as the bacteriophage T4-encoded Gp31 cochaperone (van der Vieset al. 1994) or the bacteriophage RB49-encoded CocO cochaperone (Ang et al. 2000, 2001). Apparently, the bacteriophage-encoded cochaperones are uniquely qualified to help in the folding of the major bacteriophage-encoded capsid protein, Gp23 (Laemmliet al. 1970; Georgopouloset al. 1972; van der Vieset al. 1994; Andreadis and Black 1998; Anget al. 2000). Yet, Gp31 and CocO can also help GroEL in its generalized chaperone function, since either can substitute ...
Recently, we discovered and studied the first virus-encoded chaperonin of bacteriophage EL Pseudomonas aeruginosa, gene product (gp) 146. In the present work, we performed bioinformatics analysis of currently predicted GroEL-like proteins encoded by phage genomes in comparison with cellular and mitochondrial chaperonins. Putative phage chaperonins share a low similarity and do not form a monophyletic group; nevertheless, they are closer to bacterial chaperonins in the phylogenetic tree. Experimental investigation of putative GroEL-like chaperonin proteins has been continued by physicochemical and functional characterization of gp246 encoded by the genome of Pseudomonas fluorescens bacteriophage OBP. Unlike the more usual double-ring architecture of chaperonins, including the EL gp146, the recombinant gp246 produced by E. coli cells has been purified as a single heptameric ring. It possesses an ATPase activity and does not require a co-chaperonin for its functioning. In vitro experiments ...
TY - JOUR. T1 - Interactions of GroEL/GroES with a heterodimeric intermediate during α2β2 assembly of mitochondrial branched-chain α-ketoacid dehydrogenase. T2 - cis capping of the native-like 86-kDa intermediate by GroES. AU - Song, Jiu Li. AU - Wynn, R. Max. AU - Chuang, David T.. PY - 2000/7/21. Y1 - 2000/7/21. N2 - We showed previously that the interaction of an αβ heterodimeric intermediate with GroEL/GroES is essential for efficient α2β2 assembly of human mitochondrial branched-chain α-ketoacid dehydrogenase. In the present study, we further characterized the mode of interaction between the chaperonins and the native-like αβ heterodimer. The αβ heterodimer, as an intact entity, was found to bind to GroEL at a 1:1 stoichiometry with a K(D) of 1.1 x 10-7 M. The 1:1 molar ratio of the GroEL-αβ complex was confirmed by the ability of the complex to bind a stoichiometric amount of denatured lysozyme in the trans cavity. Surprisingly, in the presence of MgADP, GroES was able to cap ...
In the present study, we showed that the presence of an elevated level of IgA antibodies against human Hsp60 protein predicts a coronary event several years before the coronary event actually occurs. Researchers at Wicks laboratory have studied the role of microbial Hsp60 in the development of atherosclerosis. Their studies indicate that immunization with mycobacterial Hsp65 induces atherosclerosis in laboratory animals.3,4⇓ In humans, they have found that immunity to mycobacterial Hsp65 is associated with the pathogenesis of carotid5 and coronary6 atherosclerosis. Hsp65 antibodies were found more often in patients with atherosclerotic lesions than in persons without such lesions,5 and the presence of these antibodies also predicted carotid atherosclerosis.7,8⇓ It has been shown that these antibodies cross-react with E coli Hsp60, chlamydial Hsp60, and human Hsp60 antibodies and are cytotoxic to endothelial cells.9 In the present study, we confirmed these findings and extended them to apply ...
Email: [email protected] Tom received his BS degree in Bacteriology from the University of Wisconsin-Madison in 1983. He worked as a research technician at UW-Madison in the lab of Norman Drinkwater (McArdle Laboratory for Cancer Research) until entering graduate school in 1985. He did graduate work in the laboratory of Costa Georgopoulos at the University of Utah in Salt Lake City and was awarded a PhD. degree in 1991. His thesis work focused on the role of E. coli heat shock proteins GroEL and GroES in bacteriophage morphogenesis. He returned to UW-Madison for post-doctoral work in the Craig lab, (supported by a fellowship from the National Institutes of Health), where he primarily studied the biochemistry of the SSA and SSB cytosolic Hsp70 chaperones of S. cerevisiae. In 1995, he became an associate researcher in the Plant Biotechnology Lab at the UW Biotechnology Center. The primary focus of his work at the UWBC was the expression and characterization of microbial enzymes in transgenic ...
Heat shock 10 kDa protein 1 (Hsp10) also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF) is a protein that in humans is encoded by the HSPE1 gene. The homolog in E. coli is GroES that is a chaperonin which usually works in conjunction with GroEL. GroES exists as a ring-shaped oligomer of between six and eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides an isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60. Escherichia coli GroES has also been shown to bind ATP cooperatively, and with an affinity comparable to that of GroEL. Each GroEL subunit ...
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PRIMARY OBJECTIVES:. I. To estimate the maximum tolerated dose (MTD) and clinically appropriate dose of human heat shock protein (hsp)110-gp100 chaperone complex melanoma vaccine (recombinant hsp110-gp100 chaperone complex vaccine) to recommend a phase II dose in stage IIIB/C and stage IV metastatic melanoma patients.. SECONDARY OBJECTIVES:. I. To examine the effect of the recombinant human hsp110-gp100 chaperone complex vaccine on measurable clinical tumor.. II. To determine gp100 and hsp110 specific cell mediated and humoral immune responses elicited by the chaperone complex vaccine.. III. To determine the effect of dose and serial administration of the chaperone complex vaccine on cell mediated and humoral immune responses.. IV. To quantify patient characteristics (human leukocyte antigen [HLA] subtype, immune cell function, etc.) that may correlate with immune response to the chaperone complex vaccine.. OUTLINE: This is a dose-escalation study.. Patients receive recombinant hsp110-gp100 ...
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A new study reveals that the static snapshots recorded in protein crystallography may be missing the bigger picture. Investigations of a bacterial protein using cryomicroscopy shows the protein in a balloon-like mode previously hidden from sold state studies. The discovery suggests that techniques complementary to X-ray crystallography are essential if molecular biology is to gain a complete understanding of protein structure.. Steven Ludtke, assistant professor of biochemistry and molecular biology and co-director of the National Center for Macromolecular Imaging at Baylor College of Medicine and colleagues Dong-Hua Chen and Wah Chiu there and Jiu-Li Song and David Chuang at The University of Texas Southwestern Medical Center in Dallas, studied a mutant protein and came to this perhaps not so startling conclusion. The protein GroEL chaperones misfolded proteins and nudges them into their active folded state in the cell. Protein misfolding is implicated in a number of neurodegenerative diseases, ...
The gene encoding a highly immunogenic mycobacterial heat-shock protein (hsp65) was transfected into the murine macrophage tumor cell line J774. The resulting hsp65-expressing cells (J774-hsp65) were no longer able to produce tumors in syngeneic mice. This loss of tumorigenicity was not mediated through T cells since the transfected cells did not produce tumors in athymic mice. If mice are first immunized with the J774-hsp65 cells and then challenged with the parent J774 cells, the mice do not develop tumors, indicating that the presence of the mycobacterial hsp65 protein greatly enhances immunological recognition of unique structures expressed by the parent tumor cells. This is further confirmed by the demonstration in vitro of T cells derived from J774-hsp65-immunized mice that are cytotoxic for the parent J774 cells. The results provide the basis for a novel strategy for enhancing the immunological recognition and decreasing the tumorigenicity of transformed cells. ...
Mycobacterial heat shock proteins have been implicated in the way the host response to mycobacterial infection is finely balanced to control pathogen dissemination while preventing immunopathology. Constitutive overexpression of mycobacterial Hsp70 (myHsp70) enhances mycobacterial clearance in mouse models, and Hsps can promote antitumor and antiviral immune responses. Human dendritic cells pulsed with myHsp70 generate potent antigen-specific cytotoxic T cell responses, which are dependent on a calcium-signaling cascade. Floto et al. now show that this critical function of myHsp70 is dependent on signaling through the HIV coreceptor, CCR5.. R. A. Floto, P. A. MacAry, J. M. Boname, T. S. Mien, B. Kampmann, J. R. Hair, O. S. Huey, E. N. G. Houben, J. Pieters, C. Day, W. Oehlmann, M. Singh, K. G. C. Smith, P. J. Lehner, Dendritic cell stimulation by mycobacterial Hsp70 is mediated through CCR5. Science 314, 454-458 (2006). [Abstract] [Full Text]. ...
Over the last few years, some of our experiments in which mycobacterial heat-shock protein HSP antigens were presented to the immune system as if they were viral antigens have had a significant impact on our understanding of protective immunity against tuberculosis. They have also markedly enhanced the prospects for new vaccines. We now know...
سیستمی با قرار دادن پیشبر شوک حرارتی E. coli (groE) در ناقل‌ پلاستیدی و ساخت سیگما فاکتور هیبرید گیاه- باکتری تحت یک پیشبر مختص بافت طراحی گردید تا بتوان بر مشکل کاهش رشد و یا باروری گیاه در انتقال ژن به پلاستید که اغلب به دلیل اثرات تولید دائمی محصول تراژن ایجاد می‌گردد غلبه نمود. به‌طوری‌که با ترکیب موتیف‌های قسمت پایانة N شبه سیگما فاکتور توتون که دارای توالی نشانه برای ورود به کلروپلاست و موتیف برهمکنش با پلیمراز کلروپلاستی می‌باشد با موتیف‌های قسمت C-ترمینال فاکتور سیگما 32ی E. coli که قدرت تشخیص و اتصال به پروموتر groE را دارد، یک فاکتور سیگمای هیبرید گیاه E. coli
DNA is formed from two polynucleotide chains. Each chain has a helical structure (a helix), in other words the molecule is coiled like a spring.. The two helices are then intertwined to give a double helix. The bases are on the inside of the helix and the phosphate groups are on the outside.. The two helices are held together by pairing of the nucleotides bases through hydrogen bonding. Because the double ring purines are bigger than the single ring pyrimidines the structure can only form with purine bases opposite pyrimidine bases. A big one complements a little one to take up about the same space.. ...
So to create my own "family tree" of two dozen or so microbes, I said to hell with 16S ribosomes and decided to use, as my yardstick, genetic variation in the GroEL gene, which codes for the 60-kiloDalton heat-shock protein. I chose this protein (or rather, the gene for it) as my phylo-yardstick for a number of reasons. First, the DNA sequence is sizable, at about 1643 nucleotides (making it somewhat bigger than the 16S rDNA). Its important to have a large yardstick gene when looking for faint genetic signals. Secondly, this protein is essentially universal in prokaryotes. Its ubiquitous but not necessarily highly conserved, in the same sense that rRNA is highly conserved. ("Highly conserved" is not what you want. Think about it. Taken to the extreme, a "highly conserved" sequence is invariant. It never changes. And is therefore useless for phylogenetics.) Thirdly, the GroEL heat-shock protein has multiple intracellular touchpoints: Its known to interact with GroES, ALDH2, and dihydrofolate ...
NUCLEOTIDE MONOMER. H. 5. Pyrimidines (single ring bases) thymine cytosine uracil Purines (double-ring bases) adenine guanine. 1. 5C ribose/ deoxyribose sugar @ 1 C , N-base covalently bonds @ 5 C, phosphate bonds. DEHYDRATION. l inks them. Slideshow 2227992 by...
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Hsp40 antibody [k1C7] (DnaJ (Hsp40) homolog, subfamily B, member 1) for ELISA, WB. Anti-Hsp40 mAb (GTX50059) is tested in Human samples. 100% Ab-Assurance.
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Hsp70兔多克隆抗体(ab69413)可与小鼠, 大鼠, 羊, 仓鼠, 牛, 狗, 人, 猪, 猴样本反应并经WB, IP实验严格验证。所有产品均提供质保服务,中国75%以上现货。
Hsp60兔多克隆抗体(ab82513)可与小鼠, 大鼠, 羊, 兔, 鸡, 豚鼠, 仓鼠, 牛, 狗, 人, 猪, 果蝇, 鱼, 猴, 大肠杆菌, 蟹样本反应并经WB实验严格验证,被1篇文献引用。
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The chaperonin GroEL binds non-native polypeptides in an open ring via hydrophobic contacts and then, after ATP and GroES binding to the same ring as polypeptide, mediates productive folding in the now hydrophilic, encapsulated cis chamber. The nature of the folding reaction in the cis cavity remains poorly understood. In particular, it is unclear whether polypeptides take the same route to the native state in this cavity as they do when folding spontaneously free in solution. Here, we have addressed this question by using NMR measurements of the time course of acquisition of amide proton exchange protection of human dihydrofolate reductase (DHFR) during folding in the presence of methotrexate and ATP either free in solution or inside the stable cavity formed between a single ring variant of GroEL, SR1, and GroES. Recovery of DHFR refolded by the SR1/GroES-mediated reaction is 2-fold higher than in the spontaneous reaction. Nevertheless, DHFR folding was found to proceed by the same trajectories ...
In Mycobacterium tuberculosis there are 2 distinct groEL homologues which encode the chaperonins Cpn60.1 and Cpn60.2, with the latter predicted to be the main house-keeping chaperonin. Phylogenetic analysis has revealed that the genes for the duplicated chaperonins diverged a long time ago. This implies that the duplicated chaperonins have evolved for different cellular functions. Interestingly, while most chaperonins occur as stable large complexes with a characteristic double ring structure of 14 subunits, the Mycobacterial chaperonins are very unstable and appear to form much smaller complexes. Given that the large structures formed by most chaperonins are vital to their mechanism of action, it is unclear why the oligomers are so much less stable in Mycobacteria. In this study I present detailed functional and oligomeric analysis of the M. tuberculosis chaperonins. Using various biological techniques, including complementation assays, site directed mutagenesis, and domain swap experiments; I ...
Here, we study and compare the mechanisms of action of the GroEL/GroES and the TRiC chaperonin systems on MreB client protein variants extracted from E. coli. MreB is a homologue to actin in prokaryotes. Single-molecule fluorescence correlation spectroscopy (FCS) and time-resolved fluorescence polarization anisotropy report the binding interaction of folding MreB with GroEL, GroES and TRiC. Fluorescence resonance energy transfer (FRET) measurements on MreB variants quantified molecular distance changes occurring during conformational rearrangements within folding MreB bound to chaperonins. We observed that the MreB structure is rearranged by a binding-induced expansion mechanism in TRiC, GroEL and GroES. These results are quantitatively comparable to the structural rearrangements found during the interaction of beta-actin with GroEL and TRiC, indicating that the mechanism of chaperonins is conserved during evolution. The chaperonin-bound MreB is also significantly compacted after addition of ...
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hsp18.5, heat, shock, protein, 18.5, Hsp18.5 | heat shock protein 18.5, Anti-HSP18.5 | clss IV heat shock protein ANTIBODY, O64564.1, AS11 1628
How chaperones help proteins to fold is still a matter of great debate in the scientific literature. This Classroom puzzle will help students explore different possible ways that a chaperone can interact with its client proteins. The puzzle includes a frozen chaperone protein-a miniaturized version of GroEL that can perform some of the functions of the full GroEL chaperone. The folding client is barnase, an well-behaved bacterial protein that is a popular model in protein folding studies. Players can choose to start with barnase in either the folded or unfolded state. To switch between the folded and unfolded starts, reset the puzzle (see the Actions menu in Original Interface; or the Undo menu in Selection Interface). It will be up to you to determine what provides the optimal balance between folding and interaction with the chaperone ...
Lots of the antibiotics now in use were found kind of accidentally, and their mechanisms of motion have in basic terms been elucidated after their discovery. to satisfy the clinical want for next-generation antibiotics, a extra rational method of antibiotic improvement is obviously needed.. commencing with a basic advent approximately antimicrobial medicines, their pursuits and the matter of antibiotic resistance, this reference systematically covers at the moment identified antibiotic sessions, their molecular mechanisms and the goals on which they act. Novel ambitions akin to phone signaling networks, riboswitches and bacterial chaperones are lined the following, along the newest info at the molecular mechanisms of present blockbuster antibiotics. With its large evaluate of present and destiny antibacterial drug improvement, this detailed reference is vital studying for someone taken with the improvement and healing program of novel antibiotics ...
A nitrogenous base that has a double ring structure made up of a five-atom ring attached by one side to a six-atom ring. The two rings contain a total of five carbon and four nitrogen atoms. Biologically significant purines include the bases adenine and guanine. When bound to a ribose or deoxyribose sugar and a phosphate molecule, these bases form two of the five nucleotide
MRP has released a new carbon fiber-enhanced version of its AMG single-ring chainguide, dropping the weight from around 125g down to
TY - JOUR. T1 - αB-crystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers. AU - Iwaki, T.. AU - Iwaki, A.. AU - Tateishi, J.. AU - Sakaki, Y.. AU - Goldman, J. E.. PY - 1993/12/1. Y1 - 1993/12/1. N2 - To understand the significance of the accumulation of αB-crystallin in Rosenthal fibers within astrocytes, the expression and metabolism of αB- crystallin in glioma cell lines were examined under the conditions of heat and oxidative stress, αB-crystallin mRNA was increased after both stresses, and αB-crystallin protein moved from a detergent-soluble form. In addition, Western blotting of Alexanders disease brain homogenates revealed that the 27-kd heat shock protein (HSP27), which is related to αB-crystallin, accumulates along with αB-crystallin. The presence of HSP27 in Rosenthal fibers was directly demonstrated by immunohistochemistry. Our results suggest that astrocytes in Alexanders disease may be ...
The substrate recognition mechanisms in chaperonins Chaperonins are a family of proteins devoted to assisting the folding of other proteins. They are large oligomers assembled into ring structures that enclose a cavity in which folding takes place. For this process to occur, the chaperonin must first recognize and interact with the unfolded polypeptide, then undergo a conformational change upon nucleotide binding that results in the closure of the cavity which in turn mediates the folding reaction inside the cavity. Although this general mechanism seems to apply to every chaperonin studied so far, there exist two different modes of interaction between the chaperonin and the substrate. The first occurs mainly through the interaction between the exposed hydrophobic residues of the unfolded polypeptides and those of the chaperonin substrate binding site, as elucidated for the chaperonin GroEL from E. coli. The second type of mechanism has been described so far only for the cytosolic chaperonin CCT ...
Monoclonal antibodies to the human homologue of the bacterial 65 kD heat shock protein (hsp) were used to investigate the tissue distribution of endogenous hsp 65 in normal versus rheumatoid synovial tissue, in subcutaneous nodules of patients with rheumatoid arthritis (RA) and in several instances of non-rheumatoid inflammation. A strong reactivity of the anti-hsp antibody was found in the cartilage-pannus junction in rheumatoid joints and in rheumatoid nodules, but not in normal joints or in normal or inflamed kidney or liver (irreversible graft rejection, chronic glomerulonephritis or primary biliary cirrhosis). The findings provide a new hypothetical explanation for a role of T cells reactive with the 65 kD hsp in the generation of both articular and extra-articular lesions in chronic rheumatoid arthritis.
Implant infections are a major complication in the field of orthopaedics. Bacteria attach to the implant-surface and form biofilm-colonies which makes them difficult to treat. Not only immune cells exclusively respond to bacterial challenges, but also local tissue cells are capable of participating in defense mechanisms. The aim of this study was to evaluate the role of osteoblasts in the context of implant infections. Primary osteoblasts were cultivated and stimulated with free-swimming bacteria at 4 °C and 37 °C. Supernatants were harvested for ELISA and expression of pro-inflammatory cytokines evaluated by RT-PCR. Bacterial binding to osteoblasts was evaluated using cytofluorometry and uptake was investigated by 3H thymidine-labelling of bacteria. Osteoblasts were additionally stimulated with the extracellular polymeric substance (EPS) of Staphylococcus epidermidis biofilms, as well as components of the EPS; the bacterial heat shock protein GroEL in particular. We demonstrated that binding of
Implant infections are a major complication in the field of orthopaedics. Bacteria attach to the implant-surface and form biofilm-colonies which makes them difficult to treat. Not only immune cells exclusively respond to bacterial challenges, but also local tissue cells are capable of participating in defense mechanisms. The aim of this study was to evaluate the role of osteoblasts in the context of implant infections. Primary osteoblasts were cultivated and stimulated with free-swimming bacteria at 4 °C and 37 °C. Supernatants were harvested for ELISA and expression of pro-inflammatory cytokines evaluated by RT-PCR. Bacterial binding to osteoblasts was evaluated using cytofluorometry and uptake was investigated by 3H thymidine-labelling of bacteria. Osteoblasts were additionally stimulated with the extracellular polymeric substance (EPS) of Staphylococcus epidermidis biofilms, as well as components of the EPS; the bacterial heat shock protein GroEL in particular. We demonstrated that binding of
Fullerenes are spherical molecular structures made of a single carbon layer. The most famous fullerene is the C60, a football-shaped object of 60 carbon atoms. Despite these molecules being of technological relevance, for example in organic solar cells and medical research, chemists find it difficult to tinker with fullerenes, because they dissolve only in a few toxic solvents.. Now, solvation scientist Guido Clever from TU Dort-mund University and colleagues from Nagasaki University, Japan, describe supramolecular cage- and bowl-like structures that can host fullerenes and dissolve them in many more solvents. Their results have been published on 8 May 2019 in the online edition of the Journal of the American Chemical Society.. "In this paper we show how to solubilize notoriously insoluble fullerenes in a number of polar organic solvents which then allows chemical modification of the fullerenes", says Clever. To demonstrate the new approach towards the solvation of fullerenes, the Clever Lab ...
Principal Investigator:KUWAJIMA Kunihiro, Project Period (FY):2008 - 2012, Research Category:Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area), Project Area:Molecular Science of Fluctuations toward Biological Functions
Posted by Vesa Raiskila on December 07, 1999 at 19:45:34:. Re the polarity issue: I originally thought that getting the polarity right between the two magnets in each pair was the only thing that mattered. I didnt think that, after the rings had been correctly constructed, it mattered which side up one kept the rings around the fingers.. If you think this is important, I think you should emphasize it on the page where the instructions are. (You do emphasize it, but please read on.) Although the "inter-ring" alignment is shown correctly in the diagram, some people might think that the inter-ring aligment shown is coincidental and that the only important thing is to get the *intra-ring* polarities right. That was also the way in which I interpreted your polarity warning: I though that it concerned (only) the way in which each pair was to be assembled.. Do you have a theory of why North needs to be on the top of the right finger and South on the top of the left finger? In other words, why is it ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Escherichia coli is transformed from a commensal organism into a pathogen by acquisition of genetic elements called pathogenicity islands (PAIs). Katsowich et al. investigated how the PAI virulence genes of enteropathogenic E. coli (EPEC) respond when the bacterium attaches to a host gut cell. EPEC first sticks to the host by means of pili and then uses a PAI-encoded type 3 secretion system (T3SS) to inject multiple effectors into the host cell. But not all virulence mediators are injected. For example, CesT, a bacterial chaperone, delivers virulence effectors into the T3SS apparatus. Then, within the bacterial cytoplasm, it interacts with a gene repressor called CsrA, which reprograms bacterial gene expression to help the bacteria to adapt to epithelial cell-associated life.. Science, this issue p. 735 ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
plant Hsp101 antibody, plant heat stress antibodies, heat shock protein antibody, Anti-Hsp101 (maize) antibody, Q9S822, AS08 290Hsp101/ClpB is a member of HSP100 protein family. These proteins help protein aggregates formed during heat stress to fall apar
Anti-HSP60 polyclonal antibody (STJ93621) was developed using a synthesized peptide derived from the C-terminal region of human HSP60 at AA range: 480-560. This antibody is applicable for use in western blot, immunohistochemistry, immunofluorescence and E
In 2007, Gibson Memphis introduced the ES-339 with all the class and confidence of the classic ES-335, only a slightly smaller body. Now, with the success of the ES-339 comes the next evolution, the ES-349. Capturing the preferred features of the Historic ES-345, the 2015 ES-349 is a Walnut-finished beauty with gold hardware, Kluson Double Ring tuners, rolled neck binding, and MHS Humbuckers for maximum tone. Only 50 will be made in this Limited Run, so get yours before they are all gone.
To understand what happened next, you have to know a little about mitochondrial DNA (mtDNA). Mitochondrial DNA is contained in small, football-shaped inclusions outside the nucleus of a cell. Its widely believed that mitochondria were once independent bacteria that invaded primitive cells millions of years ago. Instead of being digested, these bacteria took up residence…
|strong|Rat anti CCTeta antibody, clone PK/16/8/a|/strong| recognizes the eta polypeptide of the CCT chaperonin molecule complex.CCTη is a 543 amino acid ~60 kDa molecule encoded by the CCT7 …
Ive kept them on the TT bike 54/42 or sometimes just the 54 as a single ring. I like them for this application and think their main help is to push me over rises/small hills a little better and thus give a better time. FYI my CP20 is about 5-8Ws higher on the o symetrics too, but my preferred cadence at threshold is 88-91. so quite slow. I do all my intervals on the turbo on the TT bike with them so that their is no big shock at the start of the year, both in physical TT position and with the rings. I race TTs competitively in the UK ...
CESK1 antibody (chaperonin containing TCP1, subunit 8 (theta)-like 2) for IHC-P, WB. Anti-CESK1 pAb (GTX117858) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
Affiliation:鳥取大学,大学院工学研究科,准教授, Research Field:Structural biochemistry,Structural biochemistry,Biophysics, Keywords:シャペロニン,分子シャペロン,αシヌクレイン,GroEL,アミロイド線維,コンフォメーション変化,機能発現機構,GroE,GroES,フォールディング, # of Research Projects:19, # of Research Products:98
PCR assay of the groEL gene for detection and differentiation of Bacillus cereus group cells. part 2 Combined immunomagnetic separation-molecular beacon-reverse transcription-PCR assay for detection of hepatitis A virus from environmental samples
The heat shock protein response appears to be triggered primarily by nonnative proteins accumulating in a stressed cell and results in increased expression of heat shock proteins (HSPs). Many heat sho
Heat shock proteins are synthesized in response to increased growth temperatures and other stress factors in virtually all organisms. The analysis of the molecular mechanism of Hsps has so far been focused mostly on the ATP‐dependent Hsp70 and GroE families, whereas the function of the members of the ATP‐independent group of small Hsps is still poorly understood.. While the expression of Hsps is ubiquitous and a similar set of proteins is produced from prokaryotes to mammals, the importance and apparent function of the different Hsps seem to vary in different organisms (Parsell and Lindquist, 1994). In yeast, thermotolerance is conveyed predominantly by Hsp104, whereas in Drosophila Hsp70 seems to be the important factor. Finally, GroE is essential for protein folding in prokaryotes and organelles; however, a functional counterpart seems to be lacking in the eukaryotic cytosol, since the structurally related TCP‐1 complex appears to be restricted to actin and tubulin folding (Lewis et al., ...
Carbon, hydrogen, oxygen, nitrogen, and phosphorous act as the building blocks for nucleic acids. In humans, nucleic acids appear as DNA and RNA, the blueprints of a persons genetics.
The immune response to C. trachomatis not only is critical to the resolution of infection but also may be responsible for disease progression. Because of this dichotomy, it is imperative to understand the nature and substance of the anti-Chlamydiaimmune response and how it differs during a mild infection and during chronic inflammation with severe consequences. The precise mechanisms that lead to immunopathology and consequent organ dysfunction in humans remains largely unknown; however, identification of the antigens associated with immunopathology is a crucial step in understanding these processes. Ultimately the development of a safe and effective vaccine or a serological test to determine probable risk of developing disease sequelae will depend on understanding the interplay between chlamydial antigens and the host immune responses that evoke protection or pathology.. We have evaluated the human immune response to chlamydial Hsp10 and assessed the potential of that immune response to be a ...
Stress proteins or heat-shock proteins (HSP) are evolutionary conserved proteins present in every prokaryotic and eukaryotic cell. Their main function is to protect cells and proteins from damage under stressful circumstances. The latter circumstances do include the cell and protein damaging effects of inflammation. The discovery of mycobacterial HSP60 being a critical antigen in the model of adjuvant arthritis, has led to studies that showed the immuno-dominance of microbial HSP60 and the potential of the microbial HSP induced repertoire of antibodies and T cells to cross-recognize the self-HSP homologues of stressed cells. Since then, the research in the immunology of stress proteins started to comprise a widening spectrum of topics with potential medical relevance. Interestingly, since stress proteins have their activities in both innate and adaptive immunity, they are key elements in the cross-roads between both arms of the immune system. Stress proteins
Smith, Edward R, Ford, Martin L, Tomlinson, Laurie A, Weaving, Gary, Rocks, Bernard F, Rajkumar, Chakravarthi and Holt, Stephen G (2011) Instability of fibroblast growth factor-23 (FGF-23): implications for clinical studies. Clinica Chimica Acta, 412 (11-12). pp. 1008-1011. ISSN 1873-3492 Smith, Edward R, Ford, Martin L, Tomlinson, Laurie A, Rocks, Bernard F, Rajkumar, Chakravarthi and Holt, Stephen G (2010) Poor agreement between commercial ELISAs for plasma fetuin-A: an effect of protein glycosylation? Clinica Chimica Acta, 411 (17-18). pp. 1367-1370. ISSN 0009-8981 Shams, Sedigheh, Shafi, Shahida, Bodman-Smith, Kikki, Williams, Peter, Mehta, Sweta and Ferns, Gordon A (2008) Anti-heat shock protein-27 (Hsp-27) antibody levels in patients with chest pain: association with established cardiovascular risk factors. Clinica Chimica Acta, 395 (1-2). pp. 42-46. ISSN 0009-8981 ...
Mouse Monoclonal Anti-HSP60 Antibody (GROEL/730) [Alexa Fluor® 700]. Mitochondrial Marker. Validated: WB, ELISA, Flow, ICC/IF, IHC-Fr, IHC-P, IP. Tested Reactivity: Human. 100% Guaranteed.
The protein folding of a nascent polypeptide is the decoding of the linear information contained in the primary sequence into the native and functionally active three‐dimensional conformation
CHEMISTS have made a solid that consists almost entirely of the football-shaped molecule buckminsterfullerene. The molecule, which contains 60 carbon atoms, was discovered in 1985 by Harry Kroto of the University of Sussex. But, until now, no one has managed to make enough of the molecules to test theories of how the bulk material should …
Complete information for CLPB gene (Protein Coding), ClpB Homolog, Mitochondrial AAA ATPase Chaperonin, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
CCT7 - CCT7 (Myc-DDK-tagged)-Human chaperonin containing TCP1, subunit 7 (eta) (CCT7), transcript variant 3 available for purchase from OriGene - Your Gene Company.
1999 10 14.367572 01 57 51.86 +14 52 33.9 22.5V 10TT191 645 C~2POO 1999 10 14.368401 01 57 51.86 +14 52 33.9 22.2V 10TT191 645 C~2POO 1999 10 14.370889 01 57 51.87 +14 52 33.8 22.5V 10TT191 645 C~2POO 2007 11 14.467276 03 00 00.13 +18 42 47.4 10TT191 568 C~1tfI 2007 11 15.413367 02 59 54.05 +18 42 20.1 10TT191 568 C~1tfI 2007 11 15.415838 02 59 54.03 +18 42 20.3 10TT191 568 C~1tfI 2010 10 09.46094 03 28 22.78 +20 06 24.3 23.4w 10TT191 F51 C~1tfI 2010 10 09.47656 03 28 22.70 +20 06 24.0 23.4w 10TT191 F51 C~1tfI 2010 11 07.48047 03 25 33.87 +19 56 04.9 23.2w 10TT191 F51 C~1tfI 2010 11 07.49219 03 25 33.78 +19 56 04.3 22.9w 10TT191 F51 C~1tfI 2010 11 07.50781 03 25 33.70 +19 56 04.1 23.3w 10TT191 F51 C~1tfI 2010 11 07.52344 03 25 33.60 +19 56 03.7 23.2w 10TT191 F51 C~1tfI 2011 10 24.54297 03 35 21.60 +20 21 44.6 23.3w 10TT191 F51 C~1tfI 2011 10 24.55859 03 35 21.52 +20 21 44.2 23.5w 10TT191 F51 C~1tfI 2012 10 22.54688 03 43 48.96 +20 40 48.1 22.9w 10TT191 F51 C~1tfI 2012 10 22.55859 03 43 48.89 +20 ...
Radiation-induced oxidation of guanine bases produces 8-oxo-7-hydro-guanine (GO). The undamaged strand (left, top) replicates normally and reproduces the standard allele (bottom). The GO base in the damaged strand (middle) pairs with an A during replication of the new strand (grey). Note that this pairs two double-ring purines. Replication of the A strand in the next round of replication results in a C ...
Aggregatibacter actinomycetemcomitans GroEL Protein Promotes Conversion of Human CD4 T Cells into IFNγ IL10 Producing Tbet Th1 Cells. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Alami M, Trescher D, Wu LF, Muller M. 2002. Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli. J Biol Chem 277(23):20499-503. Amrein KE, Takacs B, Stieger M, Molnos J, Flint NA, Burn P. 1995. Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL. Proc. Natl. Acad. Sci. USA 92:1048-1052. Andersen JB, Sternberg C, Poulsen LK, Bjorn SP, Givskov M, Molin S. 1998. New unstable variants of green fluorescent protein for studies of transient gene expression in bacteria. Appl Environ Microbiol 64 (6):2240-6. Battistoni A, Carri MT, Steinku¨hler C, Rotilio G. 1993. Chaperonins dependent increase of Cu,Zn superoxide dismutase production in Escherichia coli. FEBS Lett. 322:6-9. Berks BC. 1996. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22, 393-404. Berks BC, Palmer ...
A method of removing at least one single ring aromatic hydrocarbon from a hydrocarbon contaminated fluid. The method includes contacting the hydrocarbon contaminated fluid with carbon nanotubes to adsorb the at least one single ring aromatic hydrocarbon while exposing the hydrocarbon contaminated fluid and the carbon nanotubes to UV irradiation from at least one UV light source, preferably a UV light emitting diode (LED), with a wavelength of about 315-415 nm, preferably about 365 nm, to form a treated fluid having a reduced concentration of the at least one single ring aromatic hydrocarbon relative to the hydrocarbon contaminated fluid.
Although "heat shock proteins" are best characterized in associated with temperature, mounting evidence suggests that heat shock proteins are expressed and play vital roles during many types of cell stress. Heat shock proteins work by helping other proteins fold properly and have been classified in a functional category of proteins called molecular chaperones. Molecular chaperones catalyze the folding of a newly-translated peptide into the secondary and tertiary structures that characterize the mature protein product. Improperly-folded proteins are unstable, prone to aggregation, and dysfunctional. Correct protein folding is extremely important for protein and cell function. . Alterations in protein structure, including secondary and tertiary structure, lead to altered protein function. Similarly, improperly or incompletely folded proteins are likely to be dysfunctional and lead to complications for the cell. It should come as no surprise that improper protein folding in cells of the human body ...
What are the implications of the CCT-mediated actin folding mechanism for the structure and function of F-actin? Reisler & Egelman (2007) have collated many disparate observations concerning biochemical and structural properties of F-actin and argued convincingly that F-actin should not be considered to be a single state but rather a dynamic ensemble of many states. Transitions between states are probably coupled to rotations and tilts of subunits, which occur readily despite the apparently severe structural constraint of a constant axial rise of every subunit in the filament of approximately 27.3 Å. Put succinctly, in its breathing modes F-actin changes its shape more than its length.. The emerging view of time-correlated motions and protein function is that active enzymatic or ligand-binding states reflect configurations that pre-exist in the ensemble. In adenylate kinase, the catalytically competent closed state is occasionally sampled on microseconds-milliseconds time scales even in the ...
Related to free radical independent signaling pathways and ferredoxin [2Fe-2S] can undergo conversion to the active [4Fe-4S]2+ form of the protein by the expansion of a polymorphic and unstable GAA triplet repeat Yfh1 mediates iron use by ferrochelatase(+) (see 177000) representative of the disease state in the FXN gene and ferrochelatase (see 177000) deficiency in…
To "hit only one ring"? What is that? Sweet uses the Hegelian dialectic at least twice in this list, once when he accuses Christians of not reaching out to the poor or the rich, and again when he makes an indictment that the Church is only selling half truths. This is the Thesis/Antithesis way of brainwashing Christians by vilifying the past and elevating the present. But lets examine what Sweet is calling oxymoronic. Light is particle and wave, neither antinomic or oxymoronic. (The use of the repeated phrase "Can you hear the double ring" over and over again is a brainwashing technique). The argument about postmodernists not wanting an "in your face" society is also not oxymoronic. It is a clear choice, according to Sweet, that they want society OUT of their faces. On private issues, this is also not oxymoronic. It is cause and effect. It is about the media wanting to make a buck and the public crying out for more. There is nothing contradictory about this morass at all. TVs getting bigger ...
Anti-HSP60 antibody (monoclonal) - read details of MyBioSource antibodies in the SelectScience.net Antibody products and suppliers directory
IntroductionHeat shock proteins or HSPs are being synthesized under different kind of stress conditions and act as molecular chaperones for protein…
Complete information for CCT4P1 gene (Pseudogene), Chaperonin Containing TCP1 Subunit 4 Pseudogene 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
A lens shutter camera includes a distance adjusting mechanism which is operated by the rotation of a single ring in one direction as it is driven by a drive source such as a motor. A distance adjustment is performed by a movement of a movable taking lens barrel in the direction of an optical axis thereof. Rotation of the ring in the other direction operates a lens shutter mechanism to open the shutter blades. A shutter closing spring is charged by a shutter controlling electromagnet, and is enabled to close the shutter blades.
if you compare plant at ambiant temperature to plant at 10 degrees, plant at 10 degrees are going to be smaller because of stress caused by cold whitch involve regulation of growing, regulation of genetic program to be able to survive to cold temperature. exemples of this regulation are to permit synthesis of proteins and sugar who are cryoprotectant (chaperonin, ....), to change the membrane fluidity ...
How do chaperones operate in cells? For some major chaperones it is clear what they do, though mostly not how they do it. Hsp60, 70 and 100 families carry out folding, unfolding or disaggregation of proteins. Regarding mechanisms of action, we have the clearest picture of the ATP-driven mechanism of the bacterial Hsp60s, and structures of full-length Hsp70 and 90 family members are beginning to give insights into their allosteric mechanisms. Recent advances are giving an improved understanding of the nature of chaperone interactions with their non-native substrate proteins. There have also been significant advances in understanding the engagement of chaperones in preventing the formation of toxic aggregates in degenerative disease and the relationship of protein quality control to complex biological processes such as ageing.. ...
The impaired chaperonin 60 activity leads to impaired mitochondrial quality control. Two genes DDHD1 and CYP2U1 have shown ... Two mitochondrial resident proteins are mutated in HSP: paraplegin and chaperonin 60. Paraplegin is a m-AAA metalloprotease of ... Symptoms of HSP may begin at any age, from infancy to older than 60 years. If symptoms begin during the teenage years or later ... 60 (8): 1045-1049. doi:10.1001/archneur.60.8.1045. PMID 12925358. Harding AE (1981). "Hereditary "pure" spastic paraplegia: a ...
1998). "Streptococcus iniae, a human and animal pathogen: specific identification by the chaperonin 60 gene identification ...
Using the chaperonin 60 gene (Cpn60), specific species of DNA sequencing can be distinguished in the ~600-bp region. It is ... Species and Phenotypically Similar Lactococcus and Vagococcus Species by Reverse Checkerboard Hybridization to Chaperonin 60 ... species and phenotypically similar Lactococcus and Vagococcus species by reverse checkerboard hybridization to chaperonin 60 ... nor does it survive heating at 60 degrees Celsius for 30 minutes. It is nonpigmented. E. malodoratus does not produce ...
Species and Phenotypically Similar Lactococcus andVagococcus Species by Reverse Checkerboard Hybridization to Chaperonin 60 ...
... this is not the case with chaperonins". It has been found that many anti-chaperonin antibodies exist and are associated with ... Chaperonin 10 aids HSP60 in folding by acting as a dome-like cover on the ATP active form of HSP60. This causes the central ... In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains ... NIH Material on HSP60 HSP60 HSP60 in Flies The Chaperonin Home Page The Protein Data Bank Enzyme Database on HSP60 HSP60 on Pub ...
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 ... Lee KH, Kim HS, Jeong HS, Lee YS (October 2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial ... Lee KH, Kim HS, Jeong HS, Lee YS (2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde ...
In archaea, the chaperonin is called the thermosome. In eukarya, the chaperonin is called CCT (also called TRiC or c-cpn). ... The active chaperonin role is in turn involved with specific chaperonin-substrate interactions that may be coupled to ... more details... Chaperonins at the US National Library of Medicine Medical Subject Headings (MeSH) cpnDB: a chaperonin database ... The GroEL/GroES complex in E. coli is a Group I chaperonin and the best characterized large (~ 1 MDa) chaperonin complex. GroEL ...
The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between 6 and 8 identical subunits, ... TCP-1/cpn60 chaperonin family is a family of evolutionarily related proteins. This family includes members from the HSP60 ... This chaperonin complex is essential for the correct folding and assembly of polypeptides into oligomeric structures, of which ... These 'helper' molecules are referred to as molecular chaperones, a subfamily of which are the chaperonins, which include 10 ...
"Entrez Gene: CCT6A chaperonin containing TCP1, subunit 6A (zeta 1)". Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, ... This gene encodes a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ... Yokota S, Yanagi H, Yura T, Kubota H (2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a ... "Isolation of a gene encoding a chaperonin-like protein by complementation of yeast amino acid transport mutants with human cDNA ...
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 ... CCT is a group II cytosolic molecular chaperone (or chaperonin, a protein that assists in the folding of other macromolecular ... Brackley KI, Grantham J (Jan 2009). "Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle ...
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 ... CCT is a group II chaperonin, a large protein complex that assists in the folding of other proteins. CCT is formed of a double ... The actin is recognized, loaded, and delivered to the cytosolic chaperonin (CCT) in an open conformation by the inner end of ... In this way there are three species of actin in a filament: ATP-Actin, ADP+Pi-Actin and ADP-Actin.[47][60] The amount of each ...
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 ... 10 (10): 1546-60. doi:10.1101/gr.140200. PMC 310934 . PMID 11042152. Guasch A, Aloria K, Pérez R, et al. (2002). "Three- ...
Trent JD; Kagawa HK; Yaoi T; Olle E; Zaluzec NJ (1997). "Chaperonin filaments: the archaeal cytoskeleton?". Proceedings of the ... 148 (1): 352-60. PMC 216199 . PMID 7287626. Bang, C.; Schmitz, R.A. (2015). "Archaea associated with human surfaces: not to be ... 60 (2): 174-82. doi:10.1007/s00239-004-0046-3. PMID 15791728. Makarova KS; Grishin NV; Shabalina SA; Wolf YI; Koonin EV (2006 ... 29 (2-3): 151-60. doi:10.1016/0303-2647(93)90091-P. PMID 8374067. Golyshina OV; Pivovarova TA; Karavaiko GI; et al. (1 May 2000 ...
... can be found in the article for chaperonins. Chaperonins are characterized by a stacked double-ring structure and are found in ... Biological machines Chaperonin Chemical chaperones Heat shock protein Pharmacoperone Proteasome Protein dynamics Chaperome HSF1 ... Martin J, Hartl FU (February 1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proc. Natl ... Fenton WA, Horwich AL (May 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Q. Rev. Biophys. 36 (2 ...
"Chaperonin filaments: the archaeal cytoskeleton?". Proceedings of the National Academy of Sciences of the United States of ... "J. Bacteriol. 148 (1): 352-60. PMC 216199. PMID 7287626. *^ Bang C, Schmitz RA (2015). "Archaea associated with human surfaces ... 60] Di antara prokariota, struktur sel arkea paling mirip dengan bakteri gram positif, terutama karena keduanya memiliki lipid ...
Despite only 11% of sequence similarity, MSP and the N-terminus of the bacterial P-pilus associated chaperonin PapD share a ... They all have more than 60% sequence identity. Proteins with limited sequence similarity were identified in species from plants ...
Kelson TL, Ohura T, Kraus JP (1996). "Chaperonin-mediated assembly of wild-type and mutant subunits of human propionyl-CoA ... a. Carbamazepine (antiepileptic drug): significantly lowers enzyme levels in the liver b. E. coli chaperonin proteins groES and ... 255 (1): 60-65. PMID 6765947. Diacovich L, Mitchell DL, Pham H, Gago G, Melgar MM, Khosla C, Gramajo H, Tsai SC (2004). " ...
They and others found early on that a chaperonin-mediated folding reaction can be reconstituted in a test tube, and that has ... His research into protein folding uncovered the action of chaperonins, protein complexes that assist the folding of other ... Art Horwich Lab at Yale Interview with Arthur Horwich Chaperonin-Mediated Protein Folding Arthur Horwich Seminars: "Chaperone- ... Such assemblies, known as chaperonins, also exist in other cellular compartments and are essential components, mediating ...
Group 2 chaperonins are found in both the cytosol of eukaryotic cells as well as in archaea. Group 2 chaperonins also contain ... 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 ... Aug 2011). "Chaperonins: two rings for folding". Trends Biochem Sci. 36: 424-432. doi:10.1016/j.tibs.2011.05.003. PMID 21723731 ...
This gene encodes a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the ... Bakthavatsalam D, Soung RH, Tweardy DJ, Chiu W, Dixon RA, Woodside DG (Jun 2014). "Chaperonin-containing TCP-1 complex directly ... Roobol A, Holmes FE, Hayes NV, Baines AJ, Carden MJ (1995). "Cytoplasmic chaperonin complexes enter neurites developing in ... "Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta ...
Binding of GroES to the open cavity of the chaperonin induces the individual subunits of the chaperonin to rotate such that the ... GroEL belongs to the chaperonin family of molecular chaperones, and is found in a large number of bacteria. It is required for ... Chaperonin Heat shock protein GRCh38: Ensembl release 89: ENSG00000144381 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... Horwich AL, Fenton WA, Chapman E, Farr GW (2007). "Two families of chaperonin: physiology and mechanism". Annu. Rev. Cell Dev. ...
"Chaperonin filaments: the archaeal cytoskeleton?". Proceedings of the National Academy of Sciences of the United States of ... 148 (1): 352-60. PMC 216199 . PMID 7287626.. *^ Bang, C.; Schmitz, R.A. (2015). "Archaea associated with human surfaces: not to ... Whittaker, R. H. (January 1969). "New concepts of kingdoms of organisms". Science 163 (3863): 150-60. Bibcode:1969Sci...163.. ... 60] Another unique feature of Archaea is that no other known organisms are capable of methanogenesis (the metabolic production ...
"Chaperonin filaments: the archaeal cytoskeleton?". Proc. Natl. Acad. Sci. U.S.A. 94 (10): 5383-8. Bibcode:1997PNAS...94.5383T ... 60,0 60,1 60,2 Gupta R.S. (1998). "What are archaebacteria: life's third domain or monoderm prokaryotes related to gram- ... 60][62] Esta idea está apoiada en que as arqueas son resistentes a unha ampla variedade de antibióticos producidos ... principalmente por bacterias grampositivas,[58][60] e en que estes antibióticos actúan principalmente sobre xenes que ...
"Chaperonin filaments: the archaeal cytoskeleton?". Proceedings of the National Academy of Sciences of the United States of ... 148 (1): 352-60. PMC 216199 . PMID 7287626.. *^ Bang, C.; Schmitz, R.A. (2015). "Archaea associated with human surfaces: not to ... 60] The development of the nucleus occurred after the split between Bacteria and this common ancestor.[60] Although Archaea are ... 60] This led to the conclusion that Archaea and Eukarya shared a more recent common ancestor than Eukarya and Bacteria in ...
Yokota S, Yanagi H, Yura T, Kubota H (2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a ... Suppl 1: 355-60. PMID 8098743. Lopez-Fanarraga M, Avila J, Guasch A, et al. (2002). "Review: postchaperonin tubulin folding ... 150 (2): 349-60. doi:10.1083/jcb.150.2.349. PMC 2180222 . PMID 10908577. Takeoka A, Shimizu M, Horio T (2001). "Identification ...
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. doi:10.1038/ ... An area of the specimen is imaged at both zero and at high angle (~60-70 degrees) tilts, or in the case of the related method ...
3. Group II Chaperonin. In the group II chaperonins, both archaeal thermosome and eukaryotic chaperonin containing TCP-1 (CCT; ... First, group I chaperonin is composed of identical subunits and has seven subunits per ring whereas group II chaperonin is ... One of the most well-studied chaperonins is the GroEL from E. coli, and the recognition of substrate by this chaperonin has ... Although group I chaperonin (GroEL) and group II chaperonin (CCT) have double ring structure and share sequence similarities, ...
Crystal structure of chaperonin-60 from Paracoccus denitrificans.. Fukami TA1, Yohda M, Taguchi H, Yoshida M, Miki K. ... The crystal structure of chaperonin-60 from Paracoccus denitrificans (P.cpn60) has been determined at 3.2 A resolution by the ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Chaperonin 60 subunit beta 2, chloroplasticAdd BLAST. 546. Amino acid modifications. Feature key. Position(s). Description ... IPR018370. Chaperonin_Cpn60_CS. IPR001844. Chaprnin_Cpn60. IPR002423. Cpn60/TCP-1. IPR037290. Cpn60/TCP-1_sf. IPR027409. GroEL- ... IPR018370. Chaperonin_Cpn60_CS. IPR001844. Chaprnin_Cpn60. IPR002423. Cpn60/TCP-1. IPR037290. Cpn60/TCP-1_sf. IPR027409. GroEL- ... "Differential effects of co-chaperonin homologs on cpn60 oligomers.". Bonshtien A.L., Parnas A., Sharkia R., Niv A., Mizrahi I. ...
34:818-823, 1996) demonstrated that a 600-bp region of the chaperonin 60 (Cpn60) genes from various bacterial isolates could be ... Identification of Staphylococcus species and subspecies by the chaperonin 60 gene identification method and reverse ... Identification of Staphylococcus species and subspecies by the chaperonin 60 gene identification method and reverse ... Identification of Staphylococcus species and subspecies by the chaperonin 60 gene identification method and reverse ...
Pyrosequencing of the Chaperonin-60 Universal Target as a Tool for Determining Microbial Community Composition. John ... Pyrosequencing of the Chaperonin-60 Universal Target as a Tool for Determining Microbial Community Composition ... by direct sequencing of PCR-amplified cpn60 sequences and comparison to cpnDB, a chaperonin reference sequence database. J. Med ... Pyrosequencing of the Chaperonin-60 Universal Target as a Tool for Determining Microbial Community Composition ...
Consistent with the essential role of chaperonin 60 in mitochondrial biogenesis, we were unable to isolate mutants in which the ... However, transformants were isolated that exhibited differing levels of antisense inhibition of chaperonin 60 expression, ... the levels of the chaperonin 60 protein remain constant throughout the life cycle. ... The single Dictyostelium chaperonin 60 gene, hspA, was cloned, sequenced and characterized. Sequence comparisons and a three- ...
Given the high-affinity binding that we have observed in the present study and the normal cellular abundance of chaperonin 60, ... This implies that the structural elements or motifs that are recognized by chaperonin 60 and that are responsible for binary ... Binary complex formation is also reduced if the transient species that interact with chaperonin 60 are permitted to progress to ... Binary complex formation is substantially reduced if chaperonin 60 is presaturated with Rubisco-I, the folding intermediate of ...
Purchase Recombinant Streptococcus pyogenes serotype M12 60 kDa chaperonin(groL) ,partial. It is produced in Yeast. High purity ... Recommended name: 60 kDa chaperonin Alternative name(s): GroEL protein Protein Cpn60 ... Recombinant Streptococcus pyogenes serotype M12 60 kDa chaperonin(groL) ,partial. Recombinant Streptococcus pyogenes serotype ... Recombinant Streptococcus pyogenes serotype M12 60 kDa chaperonin(groL) ,partial,E.coli. ...
10 kDa chaperonin. PD1537. -. √. -. √. C. 10.0. 25.3%. 2. Q87DE1. Surface protein. PD0744. -. -. -. -. U. 203.1. 1.46%. 2. ... 60 kDa chaperonin. PD1538. -. √. -. √. C. 57.7. 6.2%. 2. Q87B34. Glyceraldehyde-3-phosphate dehydrogenase. PD1626. -. -. -. √. ...
Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is ... Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is ... Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is ... Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is ...
The hydrogenosomal chaperonins in this case are derived from those of the mitochondrion. This scenario is supported by the fact ... Abbreviation: cpn60, chaperonin 60.. Data deposition: The sequence reported in this paper has been deposited in the GenBank ... v) Finally, it is possible that the hydrogenosome is not of endosymbiotic origin and the chaperonin genes were derived from a ... There are three possible origins, not mutually exclusive, for the T. vaginalis chaperonins. They could be derived from either ...
Chaperonin 60α. At2g28000. 1.6. 21.59. 22.03. 21.89. 1.36. 1.23. R-5-P isomerase. At3g04790. 0.6/0.5. 19.37. n.d.. 19.91. n.d. ... J. Proteom. 2016, 131, 48-60. [Google Scholar] [CrossRef] [PubMed]. *Keller, M.; Simm, S.; SPOT-ITN Consortium. The coupling of ... Plant J. 2009, 60, 783-794. [Google Scholar] [CrossRef]. *Järvi, S.; Suorsa, M.; Tadini, L.; Ivanauskaite, A.; Rantala, S.; ... Proteomics analysis of the isolated chloroplasts was performed as described before [60,61]. Pre-fractionation of the proteins ...
60 kDa chaperonin. Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) ... 60 kDa chaperonin UniProtKBInterProSTRINGInteractive Modelling. 540 aa; Sequence (Fasta) 14 identical sequences 14 identical ...
Recombinant Arabidopsis thaliana Chaperonin 60 subunit beta 4, chloroplastic (CPN60B4), partial *. Molecule Name: Chaperonin 60 ...
60 kDa chaperonin 2 UniProtKBInterProSTRINGInteractive Modelling. 537 aa; Sequence (Fasta) Identical sequences: Arthrobacter sp ...
... a secreted chaperonin 60 with potent leukocyte-activating and bone resorbing activities. This organism also produces a plethora ...
Belongs to the chaperonin (HSP60) family.Curated. ,p>UniProtKB Keywords constitute a ,a href="http://www.uniprot.org/keywords"> ... Heat shock protein 60, mitochondrialAdd BLAST. 547. Amino acid modifications. Feature key. Position(s). DescriptionActions. ... 60 70 80 90 100. VDTLARAVSV TLGPKGRNVL IDQPFGSPKI TKDGVTVARS VSLKDKFENL 110 120 130 140 150. GARLVQDVAS KTNEVAGDGT TTATVLTRAI ... sp,Q09864,HSP60_SCHPO Heat shock protein 60, mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN=hsp60 PE=1 ...
... chaperonin). The encoded protein has an amino acid length of 573 and a mass of 61.1 kDa. GroEL is a member of the Chaperonin ( ... Chaperonin 60; CPN60; Heat shock protein 60; HSP-60; Hsp60; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; ... Other names include: 60 kDa heat shock protein, mitochondrial; 60 kDa chaperonin; ...
heat shock 60kDa protein 1 (chaperonin). *Heat shock protein 1 (chaperonin). *Heat shock protein 60 ... Inquiry: Im Looking for a pure HSP 60 protein as a positive control in western blot research for HSP 60 proteins. As primary ... also called mitochondrial HSP60 chaperonopathy or MitCHAP-60 disease. HLD4 is a severe autosomal recessive hypomyelinating ...
The results suggest that sugE encodes a chaperonin-related system whose composition might vary with temperature and growth ...
SPG13/chaperonin 60/heat-shock protein 60, SPG7/paraplegin; and mitochondrial ATP6); (4) myelin formation (e.g. SPG2/ ...
Similar to 60 kDa chaperonin (Protein Cpn60). 64.3. 5.60. 10. 25. 7. gi,115450022. Zn-dependent oligopeptidases. 86.5. 5.76. 9 ...
Chaperonin 60 / metabolism*. Chemokine CCL2 / metabolism*. Endothelial Cells / metabolism*. Homocysteine / chemistry. Humans. ... 0/Albumins; 0/CCL2 protein, human; 0/Chaperonin 60; 0/Chemokine CCL2; 454-28-4/Homocysteine; EC 3.4.24.-/ADAM Proteins; EC 3.4. ... Heat shock protein 60 kD. HSPD1. 200806_s_at. 2.005. Homocysteinylated albumin concentration was comparable to that detected in ... Year: 2005Human 60-kDa heat shock protein is a target autoantigen of T cells derived from atherosclerotic plaques.J ...
The bacterial chaperonin groEL is a double toroidal assembly, which together with the action of the ring-shaped oligomeric ...
  • Association of Rubisco activase with chaperonin-60beta: a possible mechanism for protecting photosynthesis during heat stress. (uniprot.org)
  • They are required for normal cell growth (as demonstrated by the fact that no temperature sensitive mutants for the chaperonin genes can be found in the temperature range 20 to 43 degrees Celsius) and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions. (wikipedia.org)
  • Detects a band of approximately 60 kDa (predicted molecular weight: 61 kDa). (abcam.com)
  • A study of the vaginal microbiome in healthy Canadian women utilizing cpn 60-based molecular profiling reveals distinct Gardnerella subgroup community state types. (gc.ca)
  • The results suggest that sugE encodes a chaperonin-related system whose composition might vary with temperature and growth phase. (nih.gov)
  • Ten libraries (five gastrointestinal tract locations from two groups of birds) of approximately 555-bp chaperonin 60 PCR products were prepared, and 10,932 cloned sequences were analyzed. (asm.org)
  • Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is dependent on interact. (nih.gov)
  • Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is dependent on interaction with cell surface CD14. (nih.gov)
  • In order to gain insight into the functional variety of the chloroplast chaperonin family members, we reconstituted β homo-oligomers from A. thaliana following their expression in bacteria and subjected them to a structure-function analysis. (deepdyve.com)
  • Multiple chaperonins in bacteria-why so many? (deepdyve.com)
  • The 60 kDa form of chaperonin is the immunodominant antigen of patients with Legionnaire's disease, and is thought to play a role in the protection of the Legionella bacteria from oxygen radicals within macrophages. (wikipedia.org)