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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/67596
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dc.contributor.authorThompson, Gloria M.-
dc.contributor.authorCano, Veridiana S.P.-
dc.contributor.authorValentini, Sandro Roberto-
dc.date.accessioned2014-05-27T11:21:00Z-
dc.date.accessioned2016-10-25T18:19:17Z-
dc.date.available2014-05-27T11:21:00Z-
dc.date.available2016-10-25T18:19:17Z-
dc.date.issued2003-12-18-
dc.identifierhttp://dx.doi.org/10.1016/S0014-5793(03)01305-X-
dc.identifier.citationFEBS Letters, v. 555, n. 3, p. 464-468, 2003.-
dc.identifier.issn0014-5793-
dc.identifier.urihttp://hdl.handle.net/11449/67596-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/67596-
dc.description.abstractThe evolutionarily conserved factor eIF5A is the only protein known to undergo hypusination, a unique posttranslational modification triggered by deoxyhypusine synthase (Dys1). Although eIF5A is essential for cell viability, the function of this putative translation initiation factor is still obscure. To identify eIF5A-binding proteins that could clarify its function, we screened a two-hybrid library and identified two eIF-5A partners in S. cerevisiae: Dys1 and the protein encoded by the gene YJR070C, named Lia1 (Ligand of eIF5A). The interactions were confirmed by GST pulldown. Mapping binding sites for these proteins revealed that both eIF5A domains can bind to Dys1, whereas the C-terminal domain is sufficient to bind Lia1. We demonstrate for the first time in vivo that the N-terminal α-helix of Dys1 can modulate enzyme activity by inhibiting eIF5A interaction. We suggest that this inhibition be abrogated in the cell when hypusinated and functional eIF5A is required. © 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.en
dc.format.extent464-468-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectDYS1-
dc.subjecteIF5A-
dc.subjectHypusination-
dc.subjectLIA1-
dc.subjectTwo-hybrid-
dc.subjectYJR070C-
dc.subjectfungal protein-
dc.subjectinitiation factor-
dc.subjectligand-
dc.subjectprotein Dys1-
dc.subjectprotein eIF5A-
dc.subjectprotein Lia1-
dc.subjectunclassified drug-
dc.subjectalpha helix-
dc.subjectamino terminal sequence-
dc.subjectbinding site-
dc.subjectcell viability-
dc.subjectenzyme activity-
dc.subjectenzyme regulation-
dc.subjectgene mapping-
dc.subjectgenetic code-
dc.subjecthypusination-
dc.subjectnonhuman-
dc.subjectpriority journal-
dc.subjectprotein analysis-
dc.subjectprotein binding-
dc.subjectprotein domain-
dc.subjectprotein function-
dc.subjectprotein interaction-
dc.subjectprotein modification-
dc.subjectprotein processing-
dc.subjectRNA translation-
dc.subjectSaccharomyces cerevisiae-
dc.subjecttranslation initiation-
dc.subjecttranslation regulation-
dc.subjecttwo hybrid system-
dc.subjectBinding Sites-
dc.subjectDNA, Complementary-
dc.subjectFungal Proteins-
dc.subjectGenes, Reporter-
dc.subjectGlutathione Transferase-
dc.subjectLigands-
dc.subjectModels, Molecular-
dc.subjectOxidoreductases Acting on CH-NH Group Donors-
dc.subjectPeptide Initiation Factors-
dc.subjectProtein Processing, Post-Translational-
dc.subjectProtein Structure, Secondary-
dc.subjectProtein Structure, Tertiary-
dc.subjectRecombinant Proteins-
dc.subjectRNA-Binding Proteins-
dc.subjectTwo-Hybrid System Techniques-
dc.titleMapping eIF5A binding sites for Dys1 and Lia1: In vivo evidence for regulation of eIF5A hypusinationen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationDepartment of Biological Sciences School of Pharmacy S. Paulo State University - UNESP, Rodovia Araraquara-Jaú, Km01, Araraquara, SP 14801-902-
dc.description.affiliationUnespDepartment of Biological Sciences School of Pharmacy S. Paulo State University - UNESP, Rodovia Araraquara-Jaú, Km01, Araraquara, SP 14801-902-
dc.identifier.doi10.1016/S0014-5793(03)01305-X-
dc.rights.accessRightsAcesso aberto-
dc.identifier.file2-s2.0-0346366826.pdf-
dc.relation.ispartofFEBS Letters-
dc.identifier.scopus2-s2.0-0346366826-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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