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Chaperonin: Co-chaperonin Interactions
2014Co-chaperonins function together with chaperonins to mediate ATP-dependent protein folding in a variety of cellular compartments. Chaperonins are evolutionarily conserved and form two distinct classes, namely, group I and group II chaperonins. GroEL and its co-chaperonin GroES form part of group I and are the archetypal members of this family of ...
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On the evolutionary origin of the chaperonins
Proteins: Structure, Function, and Bioinformatics, 2011AbstractAn analysis of the apical domain of the Group‐I and Group‐II chaperonins shows that they have structural similarities to two different protein folds: a “swivel‐domain” phosphotransferase and a thioredoxin‐like peroxiredoxin. There is no significant sequence similarity that supports either similarity and the degree of similarity based on ...
Dekker, C, Willison, KR, Taylor, WR
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The chaperonin folding machine
Trends in Biochemical Sciences, 2002Chaperonins are versatile molecular machines that assist the folding of a wide range of substrate proteins. They harness an ATPase cycle to control access of non-native proteins to hydrophobic binding sites. ATP binding promotes large conformational changes that partially bury the hydrophobic sites and initiate the binding of a co-chaperonin, creating ...
Helen R, Saibil, Neil A, Ranson
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Allosteric regulation of chaperonins
Current Opinion in Structural Biology, 2005Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling ...
Horovitz, A, Willison, KR
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CHAPERONIN FUNCTION DEPENDS ON STRUCTURE AND DISORDER IN CO-CHAPERONIN MOBILE LOOPS [PDF]
Biocomputing '99, 1998 Co-chaperonins from diverse organisms exhibit mobile loops which fold into a beta hairpin conformation upon binding to the chaperonin. GroES, Gp31, and human Hsp10 mobile loops exhibit a preference for the beta hairpin conformation in the free co-chaperonins, and the conformational dynamics of the human Hsp10 mobile loop appear to be restricted by ...
S. J. Landry +4 more
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Novel Chaperonins in a Prokaryote
Journal of Molecular Evolution, 2005Group II chaperonins belong to the Hsp60 family occurring in archaea and eukaryotes. The archaeal chaperonins build the thermosome, which is similar to the eukaryotic CCT (chaperonin-containing TCP-1). Eukaryotes have eight subunits, and up until now, it was thought that archaea had between one and three subunits, depending on the species.
Dennis L, Maeder +2 more
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The complexity of chloroplast chaperonins
Trends in Plant Science, 2013Type I chaperonins are large oligomeric protein ensembles that are involved in the folding and assembly of other proteins. Chloroplast chaperonins and co-chaperonins exist in multiple copies of two distinct isoforms that can combine to form a range of labile oligomeric structures.
Anna, Vitlin Gruber +3 more
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Assembly of Chaperonin Complexes
Molecular Biotechnology, 2001Chaperonins are a subclass of molecular chaperones that assist both the folding of newly synthesized proteins and the maintenance of proteins in a folded state during periods of stress. The best studied members of this family are the type I chaperonins, occurring in bacteria and evolutionarily derived organelles.
A R, Kusmierczyk, J, Martin
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Inside the chaperonin toolbox: theoretical and computational models for chaperonin mechanism
Physical Biology, 2009Despite their immense importance to cellular function, the precise mechanism by which chaperonins aid in the folding of other proteins remains unknown. Experimental evidence seems to imply that there is some diversity in how chaperonins interact with their substrates and this has led to a number of different models for chaperonin mechanism ...
Del, Lucent +2 more
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