Document Detail


Nonequivalence Observed for the 16-Meric Structure of a Small Heat Shock Protein, SpHsp16.0, from Schizosaccharomyces pombe.
MedLine Citation:
PMID:  23273429     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Yuya Hanazono; Kazuki Takeda; Toshihiko Oka; Tetsuya Abe; Taichi Tomonari; Nobuhiko Akiyama; Yoshiki Aikawa; Masafumi Yohda; Kunio Miki
Related Documents :
3084219 - The effects of anterior hypothalamic deafferentation on thyrotropin (tsh) biosynthesis ...
25098739 - Isoelectric focusing in a silica nanofluidic channel: effects of electromigration and e...
20573219 - How is the balance between protein synthesis and degradation achieved?
24655019 - Monofunctional stealth nanoparticle for unbiased single molecule tracking inside living...
23669359 - Biology and trafficking of atg9 and atg16l1, two proteins that regulate autophagosome f...
24555779 - Molecular calipers for highly precise and accurate measurements of single protein mecha...
864619 - Biochemical approaches to problems of cellular patterning.
15041679 - The efficiency of different salts to screen charge interactions in proteins: a hofmeist...
17050799 - Rosuvastatin increases alpha-1 microglobulin urinary excretion in patients with primary...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-12-22
Journal Detail:
Title:  Structure (London, England : 1993)     Volume:  -     ISSN:  1878-4186     ISO Abbreviation:  Structure     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-31     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101087697     Medline TA:  Structure     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Elsevier Ltd. All rights reserved.
Affiliation:
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Insights into the Aberrant Activity of Mutant EGFR Kinase Domain and Drug Recognition.
Next Document:  Not all reading disabilities are dyslexia: distinct neurobiology of specific comprehension deficits.