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


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.

SUBMITTER: Baytshtok V 

PROVIDER: S-EPMC7849044 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

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

Baytshtok Vladimir V   Fei Xue X   Shih Tsai-Ting TT   Grant Robert A RA   Santos Justin C JC   Baker Tania A TA   Sauer Robert T RT  

Cell reports 20210101 3


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<sub>6</sub> unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV<sub>12</sub> peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteo  ...[more]

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