Literature DB >> 9145101

Interaction of Hsp70 chaperones with substrates.

S Rüdiger1, A Buchberger, B Bukau.   

Abstract

Determination of the structure of the substrate binding domain of the Escherichia coli Hsp70 chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within substrates provide insights into the principles governing Hsp70 interaction with polypeptide chains. DnaK recognizes extended peptide strands composed of up to five consecutive hydrophobic residues within and positively charged residues outside the substrate binding cavity.

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Year:  1997        PMID: 9145101     DOI: 10.1038/nsb0597-342

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN: 1072-8368


  105 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.  Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity.

Authors:  E A Nollen; J F Brunsting; J Song; H H Kampinga; R I Morimoto
Journal:  Mol Cell Biol       Date:  2000-02       Impact factor: 4.272

3.  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

4.  The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands.

Authors:  P Klappa; R B Freedman; M Langenbuch; M S Lan; G K Robinson; L W Ruddock
Journal:  Biochem J       Date:  2001-03-15       Impact factor: 3.857

Review 5.  HSP90 at the hub of protein homeostasis: emerging mechanistic insights.

Authors:  Mikko Taipale; Daniel F Jarosz; Susan Lindquist
Journal:  Nat Rev Mol Cell Biol       Date:  2010-06-09       Impact factor: 94.444

6.  The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG.

Authors:  Shawn Y Stevens; Sheng Cai; Maurizio Pellecchia; Erik R P Zuiderweg
Journal:  Protein Sci       Date:  2003-11       Impact factor: 6.725

7.  UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates.

Authors:  Julio J Caramelo; Olga A Castro; Leonardo G Alonso; Gonzalo De Prat-Gay; Armando J Parodi
Journal:  Proc Natl Acad Sci U S A       Date:  2002-12-23       Impact factor: 11.205

8.  Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells.

Authors:  Harm H Kampinga; Bart Kanon; Florian A Salomons; Alexander E Kabakov; Cam Patterson
Journal:  Mol Cell Biol       Date:  2003-07       Impact factor: 4.272

9.  Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution.

Authors:  E B Bertelsen; H Zhou; D F Lowry; G C Flynn; F W Dahlquist
Journal:  Protein Sci       Date:  1999-02       Impact factor: 6.725

10.  Hsp90-Tau complex reveals molecular basis for specificity in chaperone action.

Authors:  G Elif Karagöz; Afonso M S Duarte; Elias Akoury; Hans Ippel; Jacek Biernat; Tania Morán Luengo; Martina Radli; Tatiana Didenko; Bryce A Nordhues; Dmitry B Veprintsev; Chad A Dickey; Eckhard Mandelkow; Markus Zweckstetter; Rolf Boelens; Tobias Madl; Stefan G D Rüdiger
Journal:  Cell       Date:  2014-02-27       Impact factor: 41.582

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