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dc.contributor.authorHallett, ST
dc.contributor.authorSchellenberger, P
dc.contributor.authorZhou, L
dc.contributor.authorBeuron, F
dc.contributor.authorMorris, E
dc.contributor.authorMurray, JM
dc.contributor.authorOliver, AW
dc.date.accessioned2021-07-02T11:15:09Z
dc.date.available2021-07-02T11:15:09Z
dc.identifier.citationNucleic acids research, 2021, 49 (8), pp. 4534 - 4549
dc.identifier.issn0305-1048
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4668
dc.identifier.eissn1362-4962
dc.identifier.eissn1362-4962en_US
dc.identifier.doi10.1093/nar/gkab234
dc.identifier.doi10.1093/nar/gkab234en_US
dc.description.abstractThe multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein 'holo-complex' is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase activity, binding to the head-end of the complex to suppress turnover, irrespective of the DNA-bound status of the complex.
dc.formatPrint
dc.format.extent4534 - 4549
dc.languageeng
dc.language.isoeng
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectEscherichia coli
dc.subjectSaccharomyces cerevisiae
dc.subjectCell Cycle Proteins
dc.subjectSaccharomyces cerevisiae Proteins
dc.subjectChromosomal Proteins, Non-Histone
dc.subjectDNA
dc.subjectMicroscopy, Electron, Transmission
dc.subjectAdenosine Triphosphatases
dc.titleNse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex.
dc.typeJournal Article
dcterms.dateAccepted2021-03-22
rioxxterms.versionVoR
rioxxterms.versionofrecord10.1093/nar/gkab234
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
dc.relation.isPartOfNucleic acids research
pubs.issue8
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy
pubs.publication-statusPublished
pubs.volume49en_US
pubs.embargo.termsNot known
icr.researchteamStructural Electron Microscopy
icr.researchteamStructural Electron Microscopyen_US
dc.contributor.icrauthorBeuron, Fabienneen
dc.contributor.icrauthorMorris, Edwarden


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