Mapping eIF5A binding sites for Dys1 and Lia1: In vivo evidence for regulation of eIF5A hypusination

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorThompson, Gloria M.
dc.creatorCano, Veridiana S.P.
dc.creatorValentini, Sandro Roberto
dc.date2014-05-27T11:21:00Z
dc.date2016-10-25T18:19:17Z
dc.date2014-05-27T11:21:00Z
dc.date2016-10-25T18:19:17Z
dc.date2003-12-18
dc.date.accessioned2017-04-06T01:08:08Z
dc.date.available2017-04-06T01:08:08Z
dc.identifierFEBS Letters, v. 555, n. 3, p. 464-468, 2003.
dc.identifier0014-5793
dc.identifierhttp://hdl.handle.net/11449/67596
dc.identifierhttp://acervodigital.unesp.br/handle/11449/67596
dc.identifier10.1016/S0014-5793(03)01305-X
dc.identifier2-s2.0-0346366826.pdf
dc.identifier2-s2.0-0346366826
dc.identifierhttp://dx.doi.org/10.1016/S0014-5793(03)01305-X
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/889030
dc.descriptionThe 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.
dc.languageeng
dc.relationFEBS Letters
dc.rightsinfo:eu-repo/semantics/openAccess
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 hypusination
dc.typeOtro


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