Literature DB >> 26836408

Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.

Michal Zolkiewski1, Liudmila S Chesnokova2, Stephan N Witt3.   

Abstract

Protein aggregation is a common problem in protein biochemistry and is linked to many cellular pathologies and human diseases. The molecular chaperone ClpB can resolubilize and reactivate aggregated proteins. This unit describes the procedure for following reactivation of an aggregated enzyme glucose-6-phosphate dehydrogenase mediated by ClpB from Escherichia coli in cooperation with another molecular chaperone, DnaK. The procedures for purification of these chaperones are also described.
Copyright © 2016 John Wiley & Sons, Inc.

Entities:  

Keywords:  ClpB; DnaK; molecular chaperone; protein aggregation; protein misfolding

Mesh：

Substances：

Year:  2016        PMID： 26836408      PMCID： PMC4753798          DOI： 10.1002/0471140864.ps2810s83

Source DB:  PubMed          Journal:  Curr Protoc Protein Sci        ISSN： 1934-3655


  38 in total

Review 1.  Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions.

Authors:  Arthur Horwich
Journal:  J Clin Invest       Date:  2002-11       Impact factor: 14.808

Review 2.  Molecular chaperones and protein quality control.

Authors:  Bernd Bukau; Jonathan Weissman; Arthur Horwich
Journal:  Cell       Date:  2006-05-05       Impact factor: 41.582

Review 3.  Protein aggregation and amyloidosis: confusion of the kinds?

Authors:  Frederic Rousseau; Joost Schymkowitz; Luis Serrano
Journal:  Curr Opin Struct Biol       Date:  2006-01-24       Impact factor: 6.809

Review 4.  Hsp104 and ClpB: protein disaggregating machines.

Authors:  Shannon M Doyle; Sue Wickner
Journal:  Trends Biochem Sci       Date:  2008-11-12       Impact factor: 13.807

5.  The proper ratio of GrpE to DnaK is important for protein quality control by the DnaK-DnaJ-GrpE chaperone system and for cell division.

Authors:  Shinya Sugimoto; Kozue Saruwatari; Chihana Higashi; Kenji Sonomoto
Journal:  Microbiology       Date:  2008-07       Impact factor: 2.777

Review 6.  Molecular chaperones in protein folding and proteostasis.

Authors:  F Ulrich Hartl; Andreas Bracher; Manajit Hayer-Hartl
Journal:  Nature       Date:  2011-07-20       Impact factor: 49.962

Review 7.  The molecular chaperone Hsp104--a molecular machine for protein disaggregation.

Authors:  Benjamin Bösl; Valerie Grimminger; Stefan Walter
Journal:  J Struct Biol       Date:  2006-03-06       Impact factor: 2.867

8.  Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.

Authors:  Marika Miot; Michael Reidy; Shannon M Doyle; Joel R Hoskins; Danielle M Johnston; Olivier Genest; Maria-Carmen Vitery; Daniel C Masison; Sue Wickner
Journal:  Proc Natl Acad Sci U S A       Date:  2011-04-07       Impact factor: 11.205

9.  Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB.

Authors:  Maria Nagy; Hui-Chuan Wu; Zhonghua Liu; Sabina Kedzierska-Mieszkowska; Michal Zolkiewski
Journal:  Protein Sci       Date:  2009-02       Impact factor: 6.725

10.  Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

Authors:  Maria Nagy; Izabela Guenther; Vladimir Akoyev; Micheal E Barnett; Maria I Zavodszky; Sabina Kedzierska-Mieszkowska; Michal Zolkiewski
Journal:  J Mol Biol       Date:  2009-12-01       Impact factor: 5.469
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  1 in total

1.  The Fusaric Acid Derivative qy17 Inhibits Staphylococcus haemolyticus by Disrupting Biofilm Formation and the Stress Response via Altered Gene Expression.

Authors:  Bing Wang; Chao-Rong Song; Qing-Yan Zhang; Peng-Wei Wei; Xu Wang; Yao-Hang Long; Yong-Xin Yang; Shang-Gao Liao; Hong-Mei Liu; Guo-Bo Xu
Journal:  Front Microbiol       Date:  2022-03-14       Impact factor: 5.640
  1 in total

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