FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron
Name
Molecular Microbiology - 2022 - Hari - FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an.pdf
Description
Published version
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2.12 MB
Format
Adobe PDF
Checksum (MD5)
2c5c66e3ebf70194011a8a380c3f76e6
Author(s)
Hari, Sanjay B
Morehouse, Juhee P
Baker, Tania A
Sauer, Robert T
Date Issued
December 1, 2022
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.
Version
Final published version
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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1111/mmi.15009
