Open AccessHeat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug
Author(s) -
Vladimir Baytshtok,
Fei Xue,
T. Shane Shih,
Robert A. Grant,
Justin L C Santos,
Tania A. Baker,
Robert T. Sauer
Publication year - 2021
Publication title -
cell reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.264
H-Index - 154
eISSN - 2639-1856
pISSN - 2211-1247
DOI - 10.1016/j.celrep.2020.108639
Subject(s) - proteolysis , protease , spark plug , mutant , chemistry , biophysics , degradation (telecommunications) , substrate (aquarium) , enzyme , ubiquitin , microbiology and biotechnology , biochemistry , biology , thermodynamics , physics , ecology , telecommunications , gene , computer science
SUMMARY 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 HslU 6 unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV 12 peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteolysis.
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