Chenoweth Matthew R, Trun Nancy, Wickner Sue
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
J Bacteriol. 2007 May;189(9):3635-8. doi: 10.1128/JB.01757-06. Epub 2007 Mar 2.
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.
CbpA是大肠杆菌DnaJ的同源物,可作为DnaK/Hsp70伴侣系统的辅助伴侣,其体外活性可被CbpM调节。我们发现CbpM特异性抑制CbpA的体内活性,阻止其在细胞生长和分裂中发挥作用。此外,我们已经表明,在稳定期CbpM在体内与CbpA相互作用,这表明活性抑制是相互作用的结果。这些结果揭示了大肠杆菌DnaK系统的活性在体内可被一种特异性抑制剂调节。