Literature DB >> 1879544

Supramolecular structure of the recombinant murine small heat shock protein hsp25.

J Behlke1, G Lutsch, M Gaestel, H Bielka.   

Abstract

The size and shape of the recombinant murine small heat shock protein, hsp25, have been analyzed by hydrodynamic and electron microscopic methods. According to these studies recombinant hsp25 exists in large complexes with a sphere-like shape and diameters of 15-18 nm. The molecular mass of these complexes amounts to about 730 kDa indicating that they are composed of about 32 monomers.

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Year:  1991        PMID： 1879544     DOI： 10.1016/0014-5793(91)81016-2

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  12 in total

1.  Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity.

Authors:  P Fernando; J J Heikkila
Journal:  Cell Stress Chaperones       Date:  2000-04       Impact factor: 3.667

2.  Regulation of small heat-shock proteins by hetero-oligomer formation.

Authors:  Evgeny V Mymrikov; Mareike Riedl; Carsten Peters; Sevil Weinkauf; Martin Haslbeck; Johannes Buchner
Journal:  J Biol Chem       Date:  2019-11-25       Impact factor: 5.157

3.  Molecular characterization of Oryza sativa 16.9 kDa heat shock protein.

Authors:  L S Young; C H Yeh; Y M Chen; C Y Lin
Journal:  Biochem J       Date:  1999-11-15       Impact factor: 3.857

4.  Stationary phase-associated protein expression in Mycobacterium tuberculosis: function of the mycobacterial alpha-crystallin homolog.

Authors:  Y Yuan; D D Crane; C E Barry
Journal:  J Bacteriol       Date:  1996-08       Impact factor: 3.490

5.  Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

Authors:  M Ehrnsperger; S Gräber; M Gaestel; J Buchner
Journal:  EMBO J       Date:  1997-01-15       Impact factor: 11.598

6.  The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo.

Authors:  T C Suzuki; D C Krawitz; E Vierling
Journal:  Plant Physiol       Date:  1998-03       Impact factor: 8.340

7.  Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27.

Authors:  J N Lavoie; H Lambert; E Hickey; L A Weber; J Landry
Journal:  Mol Cell Biol       Date:  1995-01       Impact factor: 4.272

8.  The Saccharomyces cerevisiae HSP12 gene is activated by the high-osmolarity glycerol pathway and negatively regulated by protein kinase A.

Authors:  J C Varela; U M Praekelt; P A Meacock; R J Planta; W H Mager
Journal:  Mol Cell Biol       Date:  1995-11       Impact factor: 4.272

9.  Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance.

Authors:  U Knauf; U Jakob; K Engel; J Buchner; M Gaestel
Journal:  EMBO J       Date:  1994-01-01       Impact factor: 11.598

10.  A novel mechanism for small heat shock proteins to function as molecular chaperones.

Authors:  Kaiming Zhang; Anastasia N Ezemaduka; Zhao Wang; Hongli Hu; Xiaodong Shi; Chuang Liu; Xinping Lu; Xinmiao Fu; Zengyi Chang; Chang-Cheng Yin
Journal:  Sci Rep       Date:  2015-03-06       Impact factor: 4.379
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