Journal
BIOCHEMISTRY
Volume 55, Issue 40, Pages 5649-5652Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00920
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Funding
- National Institutes of Health [R01 AI-016892]
- Ruth L. Kirschstein National Research Service Award [F32GM116241]
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In eubacteria, the tmRNA system frees ribosomes that stall during protein synthesis and adds an ssrA tag to the incompletely translated polypeptide to target it for degradation. The AAA+ ClpXP protease degrades most ssrA-tagged proteins in the Escherichia coli cytoplasm and was recently shown to degrade an ssrA-tagged protein in the inner membrane. However,, we find that tmRNA-mediated tagging of E. coli ProW(1-182), a different inner-membrane protein, results in degradation by the membrane-tethered AAA+ FtsH protease. ClpXP played no role in the degradation of ProW(1-182) in vivo. These studies suggest that a complex distribution of proteolytic labor maintains protein quality control in the inner membrane.
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