In Vivo Modulation of a DnaJ Homolog, CbpA, by CbpM
Author:
Affiliation:
1. Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892
2. Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JB.01757-06
Reference18 articles.
1. Growth Phase-Dependent Variation in Protein Composition of the Escherichia coli Nucleoid
2. Bird, J. G., S. Sharma, S. C. Roshwalb, J. R. Hoskins, and S. Wickner. 2006. Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein. J. Biol. Chem. 281 : 34349-34356.
3. The Hsp70 and Hsp60 Chaperone Machines
4. Chae, C., S. Sharma, J. R. Hoskins, and S. Wickner. 2004. CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM. J. Biol. Chem. 279 : 33147-33153.
5. Dumitru, G. L., Y. Groemping, D. Klostermeier, T. Restle, E. Deuerling, and J. Reinstein. 2004. DafA cycles between the DnaK chaperone system and translational machinery. J. Mol. Biol. 339 : 1179-1189.
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