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Journal of Biochemistry Advance Access published online on May 19, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp071
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

JB Minireview

Quality control of cytoplasmic membrane proteins in Escherichia coli

Yoshinori Akiyama

Institute for Virus Research, Kyoto University

Address: Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan Tel. +81-75-751-4040; Fax, +81-75-771-5699; E-Mail: yakiyama{at}virus.kyoto-u.ac.jp

Received March 31, 2009; Accepted April 11, 2009


  Abstract

In Escherichia coli, like in any organism, the cytoplasmic (inner or plasma) membrane proteins play essential roles in transport of small and macro-molecules as well as in transmission of environmental signals across the membrane. Their quality control is critically important for growth and survival of the cell. However, our knowledge about the players and mechanisms of the system is still limited. This review focuses on proteolytic quality control of membrane proteins, in which two membrane-integrated proteases, FtsH and HtpX, with different modes of action, play central roles. The prohibitin family membrane protein complexes (HflKC and QmcA) contribute to the quality control system as a regulatory factor of FtsH and also as a possible membrane-chaperone. Failure of the quality control system to function normally leads to accumulation of malfolded cytoplasmic membrane proteins, which in turn activate the stress response pathways previously believed to be specialized for sensing protein abnormalities outside the cytoplasmic membrane. In fact, many of the cytoplasmic membrane quality control factors are stress-induced. Further characterization of them as well as of the stress-sensing mechanisms would prove useful to obtain an integrated picture of the membrane protein quality control system.

Key Words: E. coli, stress responses, membrane proteases, membrane chaperones, protein degradation


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