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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/18534
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dc.contributor.authorNikolakaki, E.en
dc.contributor.authorDrosou, V.en
dc.contributor.authorSanidas, I.en
dc.contributor.authorPeidis, P.en
dc.contributor.authorPapamarcaki, T.en
dc.contributor.authorIakoucheva, L. M.en
dc.contributor.authorGiannakouros, T.en
dc.date.accessioned2015-11-24T18:53:17Z-
dc.date.available2015-11-24T18:53:17Z-
dc.identifier.issn0006-3002-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18534-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectArginine/*chemistryen
dc.subjectHumansen
dc.subjectMagnesium Chloride/chemistryen
dc.subjectMolecular Sequence Dataen
dc.subjectNuclear Proteins/chemistry/genetics/*metabolismen
dc.subjectPhosphorylationen
dc.subjectProtein Structure, Tertiaryen
dc.subjectProtein-Serine-Threonine Kinases/chemistry/genetics/metabolismen
dc.subjectRNA/chemistry/*metabolismen
dc.subjectRNA Splicingen
dc.subjectReceptors, Cytoplasmic and Nuclear/chemistry/genetics/*metabolismen
dc.subjectSerine/*chemistryen
dc.subjectTranscription Factors/chemistry/genetics/*metabolismen
dc.titleRNA association or phosphorylation of the RS domain prevents aggregation of RS domain-containing proteinsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1016/j.bbagen.2007.10.014-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/18022399-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0304416507002553/1-s2.0-S0304416507002553-main.pdf?_tid=507eee4216452585a1b49881219e9e3d&acdnat=1332915799_c72752239399b62b55113dea39fc9253-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2008-
heal.abstractDomains rich in alternating arginine and serine residues (RS domains) are found in a large number of eukaryotic proteins involved in several cellular processes. According to the prevailing view RS domains function as protein interaction domains, thereby promoting the assembly of higher-order cellular structures. Furthermore, recent data demonstrated that the RS regions of several SR splicing factors directly contact the pre-mRNA in a nonsequence specific but functionally important fashion. Using a variety of biochemical approaches, we now demonstrate that the RS domains of three proteins, not directly associated with the splicing reaction, such as lamin b receptor, acinus and peroxisome proliferator-activated receptor gamma coactivator-1 alpha, associate mainly with nuclear RNA and that this association is conducive in retaining the proteins in a soluble form. Phosphorylation by SRPK1 prevents RNA association, yet it greatly increases the fraction of the proteins recovered in soluble form, thereby mimicking the RNA effect. Based on these results we propose that the tendency to self-associate and form aggregates is a general property of RS domain-containing proteins and could be attributed to their disordered structure. RNA binding or SRPK1-mediated phosphorylation prevents aggregation and may serve to modulate the RS domain interaction modes.en
heal.journalNameBiochim Biophys Actaen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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