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          Institute: MPI für Biochemie     Collection: Cellular Biochemistry (F.-U. Hartl)     Display Documents



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ID: 41529.0, MPI für Biochemie / Cellular Biochemistry (F.-U. Hartl)
Structural plasticity and noncovalent substrate binding in the GroEL apical domain - A study using electrospray ionization mass spectrometry and fluorescence binding studies
Authors:Ashcroft, A. E.; Brinker, A.; Coyle, J. E.; Weber, F.; Kaiser, M.; Moroder, L.; Parsons, M. R.; Jager, J.; Hartl, F. U.; Hayer-Hartl, M.; Radford, S. E.
Language:English
Date of Publication (YYYY-MM-DD):2002-09-06
Title of Journal:Journal of Biological Chemistry
Journal Abbrev.:J. Biol. Chem.
Volume:277
Issue / Number:36
Start Page:33115
End Page:33126
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent crystallographic structures of apical domain constructs that show conformational plasticity in helices H and I. Additionally, ESI-MS indicates that apical domain constructs have co-populated conformations at neutral pH. To assess the ability of different apical domain conformers to bind cochaperone and substrate, model peptides corresponding to the mobile loop of GroES and to helix D from rhodanese were studied. Analysis of apical domain-peptide complexes by ESI-MS indicates that only the folded or partially folded apical domain conformations form complexes that survive gas phase conditions. Fluorescence binding studies show that the apical domain can fully bind both peptides independently. No competition for binding was observed, suggesting the peptides have distinct apical domain-binding sites. Blocking the GroES- apical domain-binding site in GroEL rendered the chaperonin inactive in binding GroES and in assisting the folding of denatured rhodanese, but still capable of binding non-native proteins, supporting the conclusion that GroES and substrate proteins have, at least partially, distinct binding sites even in the intact GroEL tetradecamer.
Comment of the Author/Creator:Date: 2002, SEP 6
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Cellular Biochemistry (F.-U. Hartl)
MPI für Biochemie/Independent Research Groups
External Affiliations:Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds LS3 9JT, W; Yorkshire, England; Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds LS3 9JT, W Yorkshire, England; Univ Leeds, Sch Biochem & Mol Sci, Leeds LS3 9JT, W Yorkshire, England
Identifiers:ISI:000177859000093 [ID No:1]
ISSN:0021-9258 [ID No:2]
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