Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug
Name
1-s2.0-S2211124720316284-main.pdf
Description
Published version
Size
2.08 MB
Format
Adobe PDF
Checksum (MD5)
453a2a0ffedd7d7e690823df27e51e0b
Author(s)
Baytshtok, Vladimir
Fei, Xue
Shih, Tsai-Ting
Grant, Robert A
Santos, Justin C
Baker, Tania A
Sauer, Robert T
Date Issued
2021
Journal
Cell Reports
Publisher
Elsevier BV
Version
Final published version
Abstract
© 2020 The Author(s) At low temperatures, protein degradation by the AAA+ HslUV protease is very slow. New crystal structures reveal that residues in the intermediate domain of the HslU6 unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV12 peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteolysis.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Creative Commons Attribution 4.0 International license
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/j.celrep.2020.108639
