Document Detail

Flexibility of GroES mobile loop is required for efficient chaperonin function.
MedLine Citation:
PMID:  22634549     Owner:  NLM     Status:  Publisher    
Chaperonin GroEL and its partner GroES assist folding of nascent and stress-damaged proteins in an ATP-dependent manner. Free GroES has a flexible "mobile loop" and binds to GroEL through the residues at tip of the loop, capping central cavity of GroEL to provide substrate polypeptide a cage for secure in-cage folding. Here, we show that restriction of flexibility of the loop by a disulfide cross-linking between cysteines within the loop results in inefficient formation of stable GroEL-polypeptide-GroES ternary complex, and inefficient folding. Then, we generated substrate proteins with enhanced binding affinity to GroEL by fusion of one or two SBP (strongly-binding-peptide for GroEL) sequences and examined the effect of disulfide cross-linking on the assisted folding. The results indicate that the higher the binding affinity of substrate polypeptide to GroEL, the more the contribution of the mobile loop flexibility to efficient in-cage folding. It is likely that the flexibility helps GroES capture GroEL's binding sites which are already occupied by substrate polypeptide with various binding modes.
Tatsuya Nojima; Takahisa Ikegami; Hideki Taguchi; Masasuke Yoshida
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-5-24
Journal Detail:
Title:  Journal of molecular biology     Volume:  -     ISSN:  1089-8638     ISO Abbreviation:  -     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-5-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012 Elsevier B.V. All rights reserved.
Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto 603-8555 Japan.
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