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The Escherichia coli DjlA and CbpA Proteins Can Substitute for DnaJ in DnaK-Mediated Protein Disaggregation

The Escherichia coli DjlA and CbpA Proteins Can Substitute for DnaJ in DnaK-Mediated Protein... The Escherichia coli DjlA and CbpA Proteins Can Substitute for DnaJ in DnaK-Mediated Protein Disaggregation Eyal Gur 1 , Dvora Biran 1 , Nelia Shechter 1 , Pierre Genevaux 2 , Costa Georgopoulos 2 , and Eliora Z. Ron 1 , * 1 Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, Israel 2 Département de Microbiologie et Médecine Moléculaire, Centre Médical Universitaire, Université de Genève, Geneva, Switzerland ABSTRACT The DnaJ (Hsp40) protein of Escherichia coli serves as a cochaperone of DnaK (Hsp70), whose activity is involved in protein folding, protein targeting for degradation, and rescue of proteins from aggregates. Two other E. coli proteins, CbpA and DjlA, which exhibit homology with DnaJ, are known to interact with DnaK and to stimulate its chaperone activity. Although it has been shown that in dnaJ mutants both CbpA and DjlA are essential for growth at temperatures above 37°C, their in vivo role is poorly understood. Here we show that in a dnaJ mutant both CbpA and DjlA are required for efficient protein dissaggregation at 42°C. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Bacteriology American Society For Microbiology

The Escherichia coli DjlA and CbpA Proteins Can Substitute for DnaJ in DnaK-Mediated Protein Disaggregation

The Escherichia coli DjlA and CbpA Proteins Can Substitute for DnaJ in DnaK-Mediated Protein Disaggregation

Journal of Bacteriology , Volume 186 (21): 7236 – Nov 1, 2004

Abstract

The Escherichia coli DjlA and CbpA Proteins Can Substitute for DnaJ in DnaK-Mediated Protein Disaggregation Eyal Gur 1 , Dvora Biran 1 , Nelia Shechter 1 , Pierre Genevaux 2 , Costa Georgopoulos 2 , and Eliora Z. Ron 1 , * 1 Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, Israel 2 Département de Microbiologie et Médecine Moléculaire, Centre Médical Universitaire, Université de Genève, Geneva, Switzerland ABSTRACT The DnaJ (Hsp40) protein of Escherichia coli serves as a cochaperone of DnaK (Hsp70), whose activity is involved in protein folding, protein targeting for degradation, and rescue of proteins from aggregates. Two other E. coli proteins, CbpA and DjlA, which exhibit homology with DnaJ, are known to interact with DnaK and to stimulate its chaperone activity. Although it has been shown that in dnaJ mutants both CbpA and DjlA are essential for growth at temperatures above 37°C, their in vivo role is poorly understood. Here we show that in a dnaJ mutant both CbpA and DjlA are required for efficient protein dissaggregation at 42°C.

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Publisher
American Society For Microbiology
Copyright
Copyright © 2004 by the American society for Microbiology.
ISSN
0021-9193
eISSN
1098-5530
DOI
10.1128/JB.186.21.7236-7242.2004
pmid
15489435
Publisher site
See Article on Publisher Site

Abstract

The Escherichia coli DjlA and CbpA Proteins Can Substitute for DnaJ in DnaK-Mediated Protein Disaggregation Eyal Gur 1 , Dvora Biran 1 , Nelia Shechter 1 , Pierre Genevaux 2 , Costa Georgopoulos 2 , and Eliora Z. Ron 1 , * 1 Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, Israel 2 Département de Microbiologie et Médecine Moléculaire, Centre Médical Universitaire, Université de Genève, Geneva, Switzerland ABSTRACT The DnaJ (Hsp40) protein of Escherichia coli serves as a cochaperone of DnaK (Hsp70), whose activity is involved in protein folding, protein targeting for degradation, and rescue of proteins from aggregates. Two other E. coli proteins, CbpA and DjlA, which exhibit homology with DnaJ, are known to interact with DnaK and to stimulate its chaperone activity. Although it has been shown that in dnaJ mutants both CbpA and DjlA are essential for growth at temperatures above 37°C, their in vivo role is poorly understood. Here we show that in a dnaJ mutant both CbpA and DjlA are required for efficient protein dissaggregation at 42°C.

Journal

Journal of BacteriologyAmerican Society For Microbiology

Published: Nov 1, 2004

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