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dc.contributor.authorTiralongo, Joe
dc.contributor.authorFujita, Akiko
dc.contributor.authorSato, Chihiro
dc.contributor.authorKitajima, Ken
dc.contributor.authorLehmann, Friederike
dc.contributor.authorOschlies, Melanie
dc.contributor.authorGerardy-Schahn, Rita
dc.contributor.authorMuenster-Kuehnel, Anja K
dc.date.accessioned2017-05-03T14:16:53Z
dc.date.available2017-05-03T14:16:53Z
dc.date.issued2007
dc.date.modified2009-05-27T08:46:12Z
dc.identifier.issn0959-6658
dc.identifier.doi10.1093/glycob/cwm064
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent783752 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherOxford University Press
dc.publisher.placeLondon
dc.publisher.urihttp://glycob.oxfordjournals.org/
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom945
dc.relation.ispartofpageto954
dc.relation.ispartofissue9
dc.relation.ispartofjournalGlycobiology
dc.relation.ispartofvolume17
dc.rights.retentionY
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode32
dc.titleThe rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme.
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by/3.0/
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomics
gro.rights.copyright© 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.
gro.date.issued2007
gro.hasfulltextFull Text
gro.griffith.authorTiralongo, Joe


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