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dc.contributor.authorHaugland, Gyri Teien
dc.contributor.authorSakakibara, N
dc.contributor.authorPey, Angel
dc.contributor.authorRollor, Clair R
dc.contributor.authorBirkeland, Nils-Kåre
dc.contributor.authorKelman, Zvi
dc.date.accessioned2016-06-07T09:05:10Z
dc.date.available2016-06-07T09:05:10Z
dc.date.issued2008-08-30
dc.PublishedNucleic Acids Research 2008, 36(17):5602-5609eng
dc.identifier.issn1362-4962en_US
dc.identifier.urihttp://hdl.handle.net/1956/12073
dc.description.abstractThe minichromosome maintenance (MCM) proteins are thought to function as the replicative helicases in archaea. In most archaeal species studied, the interaction between MCM and the initiator protein, Cdc6, inhibits helicase activity. To date, the only exception is the helicase and Cdc6 proteins from the archaeon Thermoplasma acidophilum. It was previously shown that when the Cdc6 protein interacts with MCM it substantially stimulates helicase activity. It is shown here that the mechanism by which the Cdc6 protein stimulates helicase activity is by stimulating the ATPase activity of MCM. Also, through the use of site-specific substitutions, and truncated and chimeric proteins, it was shown that an intact Cdc6 protein is required for this stimulation. ATP binding and hydrolysis by the Cdc6 protein is not needed for the stimulation. The data suggest that binding of Cdc6 protein to MCM protein changes the structure of the helicase, enhancing the catalytic hydrolysis of ATP and helicase activity.en_US
dc.language.isoengeng
dc.publisherOxford University Press (OUP)en_US
dc.rightsAttribution CC BY-NC 2.0 UKeng
dc.rights.urihttp://creativecommons.org/licenses/by-nc/2.0/ukeng
dc.titleThermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by regulating its ATPase activityen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2016-04-07T09:16:41Z
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2008 The Author(s)en_US
dc.identifier.doihttps://doi.org/10.1093/nar/gkn548
dc.identifier.cristin359764
dc.subject.nsiVDP::Matematikk og Naturvitenskap: 400en_US


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Attribution CC BY-NC 2.0 UK
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