MISC

2004年12月

Structural stability of oligomeric chaperonin 10: the role of two beta-strands at the N and C termini in structural stabilization

JOURNAL OF MOLECULAR BIOLOGY
  • Sakane, I
  • ,
  • M Ikeda
  • ,
  • C Matsumoto
  • ,
  • T Higurashi
  • ,
  • K Inoue
  • ,
  • K Hongo
  • ,
  • T Mizobata
  • ,
  • Y Kawata

344
4
開始ページ
1123
終了ページ
1133
記述言語
英語
掲載種別
DOI
10.1016/j.jmb.2004.09.082
出版者・発行元
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD

Chaperonin 10 (cpn10) is a well-conserved subgroup of the molecular chaperone family. GroES, the cpn10 from Escherichia coli, is composed of seven 10 kDa. subunits, which form a dome-like oligomeric ring structure. From our previous studies, it was found that GroES unfolded completely through a three-state unfolding mechanism involving a partly folded monomer and that this reaction was reversible. In order to study whether these unfolding-refolding characteristics were conserved in other cpn10 proteins, we have examined the structural stabilities of cpn10s from rat mitochondria (RatES) and from hyperthermophilic eubacteria Thermotoga maritima (TmaES), and compared the values to those of GroES. From size-exclusion chromatography experiments in the presence of various concentrations of Gdn-HCl at 25degreesC, both cpn10s showed unfolding-refolding characteristics similar to those of GroES, i.e. two-stage unfolding reactions that include formation of a partially folded monomer. Although the partially folded monomer of TmaES was considerably more stable compared to GroES and RatES, it was found that the overall stabilities of all three cpn10s were achieved significantly by inter-subunit interactions. We studied this contribution of inter-subunit interactions to overall stability in the GroES heptamer by introducing a mutation that perturbed subunit association, specifically the interaction between the two anti-parallel strands at the N and C termini of this protein. From analyses of the mutants' stabilities, it was revealed that the anti-parallel beta-strands at the subunit interlace are crucial for subunit association and stabilization of the heptameric GroES protein. (C) 2004 Elsevier Ltd. All rights reserved.

リンク情報
DOI
https://doi.org/10.1016/j.jmb.2004.09.082
CiNii Articles
http://ci.nii.ac.jp/naid/80017028038
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/15544816
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000225350900018&DestApp=WOS_CPL
ID情報
  • DOI : 10.1016/j.jmb.2004.09.082
  • ISSN : 0022-2836
  • CiNii Articles ID : 80017028038
  • PubMed ID : 15544816
  • Web of Science ID : WOS:000225350900018

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