Journal
RESEARCH IN MICROBIOLOGY
Volume 160, Issue 6, Pages 396-400Publisher
ELSEVIER
DOI: 10.1016/j.resmic.2009.07.002
Keywords
Cpx pathway; MalE219; Envelope stress; Proteoliposomes
Categories
Funding
- Deutsche Forschungsgemeinschaft [Hu1011/1-3]
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In Escherichia coli, the CpxRA sensor regulator system is induced by a variety of signals, including pH, osmolarity, metals and misfolded envelope proteins. Here, we analyzed the effect of the folding defective maltose binding protein MalE219 on the reconstituted Cpx signalling pathway in detail. Surprisingly, autokinase and phosphatase activities of the reconstituted CpxA-6His protein remained unaffected, whereas phosphotransfer to CpxR became activated by MalE219. Since stimulation occurred only in CpxA-containing proteoliposomes, our data provide the first biochemical indication of allosteric stimulation due to direct contact between MalE219 and the sensor kinase CpxA. Consequently, we suggest that this direct interaction is a new mechanism enabling the Cpx pathway to sense misfolded proteins. (C) 2009 Elsevier Masson SAS. All rights reserved.
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