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dc.contributor.authorFulcher, Alex J.
dc.contributor.authorSivakumaran, Haran
dc.contributor.authorJin, Hongping
dc.contributor.authorRawle, Daniel J.
dc.contributor.authorHarrich, David
dc.contributor.authorJans, DavidA.
dc.date.accessioned2019-01-18T05:11:37Z
dc.date.available2019-01-18T05:11:37Z
dc.date.issued2016
dc.identifier.issn0167-4889
dc.identifier.doi10.1016/j.bbamcr.2015.11.019
dc.identifier.urihttp://hdl.handle.net/10072/99828
dc.description.abstractThe human immunodeficiency virus (HIV)-1 transactivator protein Tat is known to play a key role in HIV infection, integrally related to its role in the host cell nucleus/nucleolus. Here we show for the first time that Tat localisation can be modulated by specific methylation, whereby overexpression of active but not catalytically inactive PRMT6 methyltransferase specifically leads to exclusion of Tat from the nucleolus. An R52/53A mutated Tat derivative does not show this redistribution, implying that R52/53, within Tat's nuclear/nucleolar localisation signal, are the targets of PRMT6 activity. Analysis using fluorescence recovery after photobleaching indicate that Tat nucleolar accumulation is largely through binding to nucleolar components, with methylation of Tat by PRMT6 preventing this. To our knowledge, this is the first report of specific protein methylation inhibiting nucleolar retention.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.relation.ispartofpagefrom254
dc.relation.ispartofpageto262
dc.relation.ispartofissue2
dc.relation.ispartofjournalBiochimica et Biophysica Acta - Molecular Cell Research
dc.relation.ispartofvolume1863
dc.subject.fieldofresearchBiological Sciences not elsewhere classified
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchMedical Microbiology
dc.subject.fieldofresearchcode069999
dc.subject.fieldofresearchcode0601
dc.subject.fieldofresearchcode1108
dc.titleThe protein arginine methyltransferase PRMT6 inhibits HIV-1 Tat nucleolar retention
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorHarrich, David


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