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dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorFujita, Akikoen_US
dc.contributor.authorSato, Chihiroen_US
dc.contributor.authorKitajima, Kenen_US
dc.contributor.authorLehmann, Friederikeen_US
dc.contributor.authorOschiles, Melanieen_US
dc.contributor.authorGerardy-Schahn, Ritaen_US
dc.contributor.authorMunster-Kuhnel, Anjaen_US
dc.date.accessioned2017-05-03T14:16:53Z
dc.date.available2017-05-03T14:16:53Z
dc.date.issued2007en_US
dc.date.modified2009-05-27T08:46:12Z
dc.identifier.issn09596658en_US
dc.identifier.doi10.1093/glycob/cwm064en_AU
dc.identifier.urihttp://hdl.handle.net/10072/17691
dc.description.abstractThe terminal sugar sialic acid (Sia) plays a pivotal role in cell-cell interaction and recognition. A prerequisite for the biosynthesis of sialoglycoconjugates is the activation of Sia to cytidine monophosphate-Sia (CMP-Sia), by CMP-Sia synthetases (CMP-Sia-syn). CMP-Sia-syn are conserved from bacteria to man, and have been found to reside in the nucleus of all vertebrate species analysed to date. We previously cloned the CMP-Sia-syn from rainbow trout (rt) and identified three clusters of basic amino acids (BC) that might act as nuclear localization signals (NLS). Here, we utilised chimeric proteins and rt CMP-Sia-syn mutants in which putative NLS sequences were deleted, to identify the nuclear transport signal. Divergent from the mouse enzyme, where the crucial NLS is part of the enzyme's active site, in the rt CMP-Sia-syn the NLS and active site are disparate. The crucial NLS in the fish enzyme is bipartite and the functionality depends on a free N-terminus. Comparative analysis of all putative rt NLS in mouse and fish cells identified a second inferior motif (rtBC5-6), which was functional only in fish cells suggesting some differences in transport mechanism or folding variabilities in fish. Moreover, based on computational analyses of putative CMP-Sia-syn from distant deuterostomian organisms it was concluded that CMP-Sia-syn nuclear localization is a relatively recent invention, originating in echinoderms. In summary, our data describing structural differences in the NLS of vertebrate CMP-Sia-syn, and the independence of Sia activation from the subcellular localization of the enzyme, provide supporting evidence that nuclear localization is linked to a second yet unknown function.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.format.extent783752 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherOxford University Pressen_US
dc.publisher.placeLondonen_US
dc.publisher.urihttp://glycob.oxfordjournals.org/en_AU
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom945en_US
dc.relation.ispartofpageto954en_US
dc.relation.ispartofissue9en_US
dc.relation.ispartofjournalGlycobiologyen_US
dc.relation.ispartofvolume17en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchcode270103en_US
dc.subject.fieldofresearchcode270108en_US
dc.titleThe rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme.en_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
dcterms.licensehttp://creativecommons.org/licenses/by/3.0/en_US
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomicsen_US
gro.rights.copyrightCopyright 2007 authors. This is an open access paper. http://creativecommons.org/licenses/by/3.0/ license that permits unrestricted use, provided that the paper is properly attributed.en_AU
gro.date.issued2007
gro.hasfulltextFull Text


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