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From Minichaperone to GroEL 3: Properties of an Active Single-ring Mutant of GroEL
Journal of Molecular Biology, 2000The next step in our reductional analysis of GroEL was to study the activity of an isolated single seven-membered ring of the 14-mer. A known single-ring mutant, GroEL(SR1), contains four point mutations that prevent the formation of double-rings. That heptameric complex is functionally inactive because it is unable to release GroES.
J, Chatellier +4 more
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1994
Abstract Both Groel and GroES are essential for growth of E. coli at all temperatures4 Temperature-sensitive, conditional lethal mutants isolated on the basis of blocking phage λgrowth show impaired DNA and RNA synthesis5, a block in cell division that results in formation of long filaments without septa at the non-permissive ...
J Martin, F -U Hartl
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Abstract Both Groel and GroES are essential for growth of E. coli at all temperatures4 Temperature-sensitive, conditional lethal mutants isolated on the basis of blocking phage λgrowth show impaired DNA and RNA synthesis5, a block in cell division that results in formation of long filaments without septa at the non-permissive ...
J Martin, F -U Hartl
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Analysis of peptides and proteins in their binding to GroEL [PDF]
Journal of Peptide Science, 2010 AbstractThe GroEL–GroES is an essential molecular chaperon system that assists protein folding in cell. Binding of various substrate proteins to GroEL is one of the key aspects in GroEL‐assisted protein folding. Small peptides may mimic segments of the substrate proteins in contact with GroEL and allow detailed structural analysis of the interactions ...
Yali, Li +3 more
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Nature and Consequences of GroEL-Protein Interactions
Biochemistry, 1995The importance of chaperonin-protein interactions has been investigated by analyzing the refolding of the barley chymotrypsin inhibitor 2 in the presence of GroEL. The chaperonin retards the rate of refolding of wild type and 32 representative point mutants.
Itzhaki, Laura S. +2 more
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GroEL and the GroEL-GroES Complex
2017Chaperonin is categorized as a molecular chaperone and mediates the formation of the native conformation of proteins by first preventing folding during synthesis or membrane translocation and subsequently by mediating the step-wise ATP-dependent release that result in proper folding.
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Structural aspects of GroEl function
Current Opinion in Structural Biology, 1998The chaperonin GroEL and its cofactor GroES facilitate protein folding in an ATP-regulated manner. The recently solved crystal structure of the GroEL.GroES.(ADP)7 complex shows that the lining of the cavity in the polypeptide acceptor state is hydrophobic, whereas in the protein-release state it becomes hydrophilic.
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Identification of in vivo substrates of the chaperonin GroEL
Nature, 1999The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that GroEL interacts strongly with a well-defined set of approximately 300 newly translated polypeptides, including essential components of the transcription/translation machinery and metabolic enzymes.
W A, Houry +4 more
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Chaperonin GroEL: Structure and Reaction Cycle
Current Protein & Peptide Science, 2007The structure of Escherichia coli chaperonin GroEL was studied using various experimental tools. Such studies produced information about its structure with increasing details. Moreover, remarkable advances in experimental methods provided a step forward in understanding the reaction cycle involved in GroEL-mediated protein folding.
K Ananda, Krishna +2 more
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Asymmetric binding of membrane proteins to GroEL
Archives of Biochemistry and Biophysics, 2005The interaction of GroEL with non-native soluble proteins has been studied intensively and structure-function relationships have been established in considerable detail. Recently, we found that GroEL is also able to bind membrane proteins in the absence of detergents and deliver them to liposomes in a biologically active state.
Jingchuan, Sun +6 more
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Sublingual Vaccine with GroEL Attenuates Atherosclerosis
Journal of Dental Research, 2014Autoimmune responses to heat-shock protein 60 (HSP60) contribute to the progression of atherosclerosis, whereas immunization with HSP60 may induce atheroprotective responses. We assessed the capacity of an atheroprotective vaccine that targeted a recombinant HSP60 from Porphyromonas gingivalis (rGroEL) to induce a protective mucosal immune response ...
M, Hagiwara +5 more
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