In vivo modulation of a DnaJ homolog, CbpA, by CbpM.
CbpA, an Escherichia coli DnaJ homolog, can function as a cochaperone for the DnaK/Hsp70 chaperone system, and its in vitro activity can be modulated by CbpM. We discovered that CbpM specifically inhibits the in vivo activity of CbpA, preventing it from functioning in cell growth and division. Furthermore, we have shown that CbpM interacts with CbpA in vivo during stationary phase, suggesting that the inhibition of activity is a result of the interaction. These results reveal that the activity of the E. coli DnaK system can be regulated in vivo by a specific inhibitor.
Chenoweth
Matthew R
MR
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Trun
Nancy
N
Wickner
Sue
S
D002352:Carrier Proteins / Q000502:physiology*; D002455:Cell Division; D004926:Escherichia coli / Q000166:cytology / Q000254:growth & development / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000502:physiology*; D017353:Gene Deletion; D015964:Gene Expression Regulation, Bacterial; D008856:Microscopy, Fluorescence; D018832:Molecular Chaperones / Q000037:antagonists & inhibitors*; D011485:Protein Binding; D013696:Temperature
D002352:Carrier Proteins; C492508:CbpM protein, E coli; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones