Literature DB >> 14731451

Partner proteins determine multiple functions of Hsp70.

J Rassow1, W Voos, N Pfanner.   

Abstract

The 70 kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that are best known for their participation in protein folding. However, evidence is accumulating that Hsp70s perform several other cellular functions in cooperation with specific soluble or membrane-bound partner proteins. While the basic function of Hsp70s is explained by their ability to bind unfolded polypeptide segments, the partner proteins appear to customize them for specific roles such as involvement in protein traffic and folding, translocation of preproteins across membranes, and gene regulation.

Entities:  

Year:  1995        PMID： 14731451     DOI： 10.1016/s0962-8924(00)89001-7

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN： 0962-8924            Impact factor:   20.808


  39 in total

1.  A chloroplast-targeted heat shock protein 70 (HSP70) contributes to the photoprotection and repair of photosystem II during and after photoinhibition.

Authors:  M Schroda; O Vallon; F A Wollman; C F Beck
Journal:  Plant Cell       Date:  1999-06       Impact factor: 11.277

2.  Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper.

Authors:  K Thress; J Song; R I Morimoto; S Kornbluth
Journal:  EMBO J       Date:  2001-03-01       Impact factor: 11.598

3.  Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role.

Authors:  T Krimmer; J Rassow; W H Kunau; W Voos; N Pfanner
Journal:  Mol Cell Biol       Date:  2000-08       Impact factor: 4.272

4.  The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria.

Authors:  Andreas Strub; Karin Röttgers; Wolfgang Voos
Journal:  EMBO J       Date:  2002-06-03       Impact factor: 11.598

5.  RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.

Authors:  M Gautschi; H Lilie; U Fünfschilling; A Mun; S Ross; T Lithgow; P Rücknagel; S Rospert
Journal:  Proc Natl Acad Sci U S A       Date:  2001-03-27       Impact factor: 11.205

Review 6.  The surprising complexity of peroxisome biogenesis.

Authors:  L J Olsen
Journal:  Plant Mol Biol       Date:  1998-09       Impact factor: 4.076

7.  The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.

Authors:  J J Silberg; K G Hoff; L E Vickery
Journal:  J Bacteriol       Date:  1998-12       Impact factor: 3.490

Review 8.  Cell wall and secreted proteins of Candida albicans: identification, function, and expression.

Authors:  W L Chaffin; J L López-Ribot; M Casanova; D Gozalbo; J P Martínez
Journal:  Microbiol Mol Biol Rev       Date:  1998-03       Impact factor: 11.056

9.  Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.

Authors:  W Voos; O von Ahsen; H Müller; B Guiard; J Rassow; N Pfanner
Journal:  EMBO J       Date:  1996-06-03       Impact factor: 11.598

10.  Characterization of Arabidopsis thaliana cDNAs that render yeasts tolerant toward the thiol-oxidizing drug diamide.

Authors:  S Kushnir; E Babiychuk; K Kampfenkel; E Belles-Boix; M Van Montagu; D Inzé
Journal:  Proc Natl Acad Sci U S A       Date:  1995-11-07       Impact factor: 11.205
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