Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.11889/2695
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dc.contributor.authorStiban, Johnny
dc.contributor.authorFarnum, Gregory
dc.contributor.authorHovde, Stacy
dc.contributor.authorKaguni, Laurie S.
dc.date.accessioned2016-10-15T08:53:33Z
dc.date.available2016-10-15T08:53:33Z
dc.date.issued2014
dc.identifier.citationen_US
dc.identifier.urihttp://hdl.handle.net/20.500.11889/2695
dc.descriptionFarnum,Gregory: Hovde,Stacy: S. Kaguni,Laurie:en_US
dc.description.abstractBackground: Despite high evolutionary conservation, the function of the N-terminal domain (NTD) of mtDNA helicase remains elusive. Results: Drosophila NTD contains an iron-sulfur cluster and binds DNA. Conclusion: The iron-sulfur cluster in mtDNA helicase enhances protein stability, and may regulate its biological functions. Significance: Discovery of an Fe-S cluster in insect mtDNA helicase presents a novel opportunity to explore species-specific relationships in the replisome.
dc.language.isoenen_US
dc.publisherAmerican Society of Biochemistry and Molecular Biologyen_US
dc.subject.lcshEvolution (Biology) -- History
dc.subject.lcshMitochondria
dc.subject.lcshIron-sulfur proteins
dc.titleThe N-terminal domain of the Drosophila mitochondrial replicative DNA helicase contains an iron-sulfur cluster and binds DNA.en_US
dc.title.alternativeen_US
dc.typeen_US
newfileds.departmenten_US
newfileds.custom-issue-dateen_US
newfileds.corporate-authoren_US
newfileds.conferenceen_US
newfileds.item-access-typeopen_accessen_US
newfileds.thesis-progen_US
newfileds.general-subjectLife Sciences and Biologyen_US
item.languageiso639-1other-
item.grantfulltextopen-
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