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dc.contributor.authorBaytshtok, Vladimir
dc.contributor.authorFei, Xue
dc.contributor.authorShih, Tsai-Ting
dc.contributor.authorGrant, Robert A
dc.contributor.authorSantos, Justin C
dc.contributor.authorBaker, Tania A
dc.contributor.authorSauer, Robert T
dc.date.accessioned2021-10-27T20:04:47Z
dc.date.available2021-10-27T20:04:47Z
dc.date.issued2021
dc.identifier.urihttps://hdl.handle.net/1721.1/134390
dc.description.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.
dc.language.isoen
dc.publisherElsevier BV
dc.relation.isversionof10.1016/j.celrep.2020.108639
dc.rightsCreative Commons Attribution 4.0 International license
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceElsevier
dc.titleHeat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug
dc.typeArticle
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biology
dc.relation.journalCell Reports
dc.eprint.versionFinal published version
dc.type.urihttp://purl.org/eprint/type/JournalArticle
eprint.statushttp://purl.org/eprint/status/PeerReviewed
dc.date.updated2021-07-13T18:43:56Z
dspace.orderedauthorsBaytshtok, V; Fei, X; Shih, T-T; Grant, RA; Santos, JC; Baker, TA; Sauer, RT
dspace.date.submission2021-07-13T18:43:58Z
mit.journal.volume34
mit.journal.issue3
mit.licensePUBLISHER_CC
mit.metadata.statusAuthority Work and Publication Information Needed


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