dc.contributor.author | Hallett, ST | |
dc.contributor.author | Schellenberger, P | |
dc.contributor.author | Zhou, L | |
dc.contributor.author | Beuron, F | |
dc.contributor.author | Morris, E | |
dc.contributor.author | Murray, JM | |
dc.contributor.author | Oliver, AW | |
dc.date.accessioned | 2021-07-02T11:15:09Z | |
dc.date.available | 2021-07-02T11:15:09Z | |
dc.date.issued | 2021-05-07 | |
dc.identifier.citation | Nucleic acids research, 2021, 49 (8), pp. 4534 - 4549 | |
dc.identifier.issn | 0305-1048 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/4668 | |
dc.identifier.eissn | 1362-4962 | |
dc.identifier.doi | 10.1093/nar/gkab234 | |
dc.description.abstract | The 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.format | Print | |
dc.format.extent | 4534 - 4549 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | OXFORD UNIV PRESS | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Escherichia coli | |
dc.subject | Saccharomyces cerevisiae | |
dc.subject | Cell Cycle Proteins | |
dc.subject | Saccharomyces cerevisiae Proteins | |
dc.subject | Chromosomal Proteins, Non-Histone | |
dc.subject | DNA | |
dc.subject | Microscopy, Electron, Transmission | |
dc.subject | Adenosine Triphosphatases | |
dc.title | Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2021-03-22 | |
rioxxterms.version | VoR | |
rioxxterms.versionofrecord | 10.1093/nar/gkab234 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Nucleic acids research | |
pubs.issue | 8 | |
pubs.notes | Not 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-status | Published | |
pubs.volume | 49 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Structural Electron Microscopy | |
icr.researchteam | Structural Electron Microscopy | |
dc.contributor.icrauthor | Beuron, Fabienne | |
dc.contributor.icrauthor | Morris, Edward | |