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dc.contributor.authorWohlever, Matthew L.
dc.contributor.authorSauer, Robert T.
dc.contributor.authorBaker, Tania
dc.date.accessioned2015-03-24T20:27:57Z
dc.date.available2015-03-24T20:27:57Z
dc.date.issued2013-11
dc.date.submitted2013-10
dc.identifier.issn0950382X
dc.identifier.issn1365-2958
dc.identifier.urihttp://hdl.handle.net/1721.1/96164
dc.description.abstractDegron binding regulates the activities of the AAA+ Lon protease in addition to targeting proteins for degradation. The sul20 degron from the cell-division inhibitor SulA is shown here to bind to the N domain of Escherichia coli Lon, and the recognition site is identified by cross-linking and scanning for mutations that prevent sul20-peptide binding. These N-domain mutations limit the rates of proteolysis of model sul20-tagged substrates and ATP hydrolysis by an allosteric mechanism. Lon inactivation of SulA in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber. Lon-mediated relief of proteotoxic stress and protein aggregation in vivo can also occur without degradation but is not dependent on robust ATP hydrolysis. In combination, these results demonstrate that Lon can function as a protease or a chaperone and reveal that some of its ATP-dependent biological activities do not require translocation.en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant AI-16982)en_US
dc.description.sponsorshipNational Science Foundation (U.S.). Graduate Research Fellowship Programen_US
dc.language.isoen_US
dc.publisherWiley Blackwellen_US
dc.relation.isversionofhttp://dx.doi.org/10.1111/mmi.12444en_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alikeen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/en_US
dc.sourcePMCen_US
dc.titleRoles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activityen_US
dc.typeArticleen_US
dc.identifier.citationWohlever, Matthew L., Tania A. Baker, and Robert T. Sauer. “Roles of the N Domain of the AAA+ Lon Protease in Substrate Recognition, Allosteric Regulation and Chaperone Activity.” Molecular Microbiology 91, no. 1 (November 10, 2013): 66–78.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.mitauthorBaker, Taniaen_US
dc.contributor.mitauthorSauer, Robert T.en_US
dc.contributor.mitauthorWohlever, Matthew L.en_US
dc.relation.journalMolecular Microbiologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsWohlever, Matthew L.; Baker, Tania A.; Sauer, Robert T.en_US
dc.identifier.orcidhttps://orcid.org/0000-0002-1719-5399
mit.licenseOPEN_ACCESS_POLICYen_US


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