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dc.contributor.authorKim, Sora
dc.contributor.authorZuromski, Kristin L
dc.contributor.authorBell, Tristan A
dc.contributor.authorSauer, Robert T
dc.contributor.authorBaker, Tania A
dc.date.accessioned2021-10-27T19:52:39Z
dc.date.available2021-10-27T19:52:39Z
dc.date.issued2020
dc.identifier.urihttps://hdl.handle.net/1721.1/133404
dc.description.abstract© Kim et al. AAA+ proteases perform regulated protein degradation in all kingdoms of life and consist of a hexameric AAA+ unfoldase/translocase in complex with a self-compartmentalized peptidase. Based on asymmetric features of cryo-EM structures and a sequential hand-over-hand model of substrate translocation, recent publications have proposed that the AAA+ unfoldases ClpA and ClpX rotate with respect to their partner peptidase ClpP to allow function. Here, we test this model by covalently crosslinking ClpA to ClpP to prevent rotation. We find that crosslinked ClpAP complexes unfold, translocate, and degrade protein substrates in vitro, albeit modestly slower than uncrosslinked enzyme controls. Rotation of ClpA with respect to ClpP is therefore not required for ClpAP protease activity, although some flexibility in how the AAA+ ring docks with ClpP may be necessary for optimal function.
dc.language.isoen
dc.publishereLife Sciences Publications, Ltd
dc.relation.isversionof10.7554/eLife.61451
dc.rightsCreative Commons Attribution 4.0 International license
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceeLife
dc.titleClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP
dc.typeArticle
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biology
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistry
dc.relation.journaleLife
dc.eprint.versionFinal published version
dc.type.urihttp://purl.org/eprint/type/JournalArticle
eprint.statushttp://purl.org/eprint/status/PeerReviewed
dc.date.updated2021-07-14T12:52:37Z
dspace.orderedauthorsKim, S; Zuromski, KL; Bell, TA; Sauer, RT; Baker, TA
dspace.date.submission2021-07-14T12:52:38Z
mit.journal.volume9
mit.licensePUBLISHER_CC
mit.metadata.statusAuthority Work and Publication Information Needed


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