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FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron

Author(s)
Hari, Sanjay B; Morehouse, Juhee P; Baker, Tania A; Sauer, Robert T
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Abstract
Targeted protein degradation plays important roles in stress responses in all cells. In E. coli, the membrane-bound AAA+ FtsH protease degrades cytoplasmic and membrane proteins. Here, we demonstrate that FtsH degrades cyclopropane fatty acid (CFA) synthase, whose synthesis is induced upon nutrient deprivation and entry into stationary phase. We find that neither the disordered N-terminal residues nor the structured C-terminal residues of the kinetically stable CFA-synthase dimer are required for FtsH recognition and degradation. Experiments with fusion proteins support a model in which an internal degron mediates FtsH recognition as a prelude to unfolding and proteolysis. These findings elucidate the terminal step in the life cycle of CFA synthase and provide new insight into FtsH function.
Date issued
2022-12-01
URI
https://hdl.handle.net/1721.1/146956
Department
Massachusetts Institute of Technology. Department of Biology
Journal
Molecular Microbiology
Publisher
Wiley
Citation
Hari, Sanjay B, Morehouse, Juhee P, Baker, Tania A and Sauer, Robert T. 2022. "FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron." Molecular Microbiology.
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