| Literature DB >> 33472065 |
Vladimir Baytshtok1, Xue Fei1, Tsai-Ting Shih1, Robert A Grant1, Justin C Santos1, Tania A Baker1, Robert T Sauer2.
Abstract
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.Entities:
Keywords: ATP-dependent degradation; heat shock locus; proteolytic regulation; temperature control
Mesh:
Substances:
Year: 2021 PMID: 33472065 PMCID: PMC7849044 DOI: 10.1016/j.celrep.2020.108639
Source DB: PubMed Journal: Cell Rep Impact factor: 9.423