PMID:15489435

Citation	Gur, E, Biran, D, Shechter, N, Genevaux, P, Georgopoulos, C and Ron, EZ (2004) The Escherichia coli DjlA and CbpA proteins can substitute for DnaJ in DnaK-mediated protein disaggregation. J. Bacteriol. 186:7236-42
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 degrees 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 degrees C.
Links	PubMed PMC523209 Online version:10.1128/JB.186.21.7236-7242.2004
Keywords	Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli/physiology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Heat-Shock Response; Mutation; Protein Denaturation/physiology; Protein Renaturation; Solubility
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