Literature DB >> 33472065

Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug.

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.
Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.

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


  22 in total

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