| Nonequivalence Observed for the 16-Meric Structure of a Small Heat Shock Protein, SpHsp16.0, from Schizosaccharomyces pombe. | |
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MedLine Citation:
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PMID: 23273429 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Small heat shock proteins (sHsps) play a role in preventing the fatal aggregation of denatured proteins in the presence of stresses. The sHsps exist as monodisperse oligomers in their resting state. Because the hydrophobic N-terminal regions of sHsps are possible interaction sites for denatured proteins, the manner of assembly of the oligomer is critical for the activation and inactivation mechanisms. Here, we report the oligomer architecture of SpHsp16.0 from Schizosaccharomyces pombe determined with X-ray crystallography and small angle X-ray scattering. Both results indicate that eight dimers of SpHsp16.0 form an elongated sphere with 422 symmetry. The monomers show nonequivalence in the interaction with neighboring monomers and conformations of the N- and C-terminal regions. Variants for the N-terminal phenylalanine residues indicate that the oligomer formation ability is highly correlated with chaperone activity. Structural and biophysical results are discussed in terms of their possible relevance to the activation mechanism of SpHsp16.0. |
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Authors:
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Yuya Hanazono; Kazuki Takeda; Toshihiko Oka; Tetsuya Abe; Taichi Tomonari; Nobuhiko Akiyama; Yoshiki Aikawa; Masafumi Yohda; Kunio Miki |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-12-22 |
Journal Detail:
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Title: Structure (London, England : 1993) Volume: - ISSN: 1878-4186 ISO Abbreviation: Structure Publication Date: 2012 Dec |
Date Detail:
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Created Date: 2012-12-31 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101087697 Medline TA: Structure Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2013 Elsevier Ltd. All rights reserved. |
Affiliation:
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Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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