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Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling

dc.contributor.authorValentini, Sandro Roberto [UNESP]
dc.contributor.authorCasolari, Jason M.
dc.contributor.authorOliveira, Carla C.
dc.contributor.authorSilver, Pamela A.
dc.contributor.authorMcBride, Anne E.
dc.contributor.institutionHarvard Medical School
dc.contributor.institutionDana-Farber Cancer Institute
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionBowdoin College
dc.date.accessioned2014-05-27T11:20:26Z
dc.date.available2014-05-27T11:20:26Z
dc.date.issued2002-03-14
dc.description.abstractThe highly conserved eukaryotic translation initiation factor eIF5A has been proposed to have various roles in the cell, from translation to mRNA decay to nuclear protein export. To further our understanding of this essential protein, three temperature-sensitive alleles of the yeast TIF51A gene have been characterized. Two mutant eIF5A proteins contain mutations in a proline residue at the junction between the two eIFSA domains and the third, strongest allele encodes a protein with a single mutation in each domain, both of which are required for the growth defect. The stronger tif51A alleles cause defects in degradation of short-lived mRNAs, supporting a role for this protein in mRNA decay. A multicopy suppressor screen revealed six genes, the overexpression of which allows growth of a tif51A-1 strain at high temperature; these genes include PAB1, PKC1, and PKC1 regulators WSC1, WSC2, and WSC3. Further results suggest that eIFSA may also be involved in ribosomal synthesis and the WSC/PKC1 signaling pathway for cell wall integrity or related processes.en
dc.description.affiliationDepartment of Biological Chemistry and Molecular Pharmacology Harvard Medical School, Boston, MA 02115
dc.description.affiliationDepartment of Cancer Biology Dana-Farber Cancer Institute, Boston, MA 02115
dc.description.affiliationDepartment of Biological Sciences School of Pharmacy São Paulo State University, Araraquara, SP, 14801-902
dc.description.affiliationDepartment of Biochemistry Institute of Chemistry University of São Paulo, São Paulo, SP 05508-900
dc.description.affiliationDana-Farber Cancer Institute, 44 Binney St., SM922, Boston, MA 02115
dc.description.affiliationDepartment of Biology Bowdoin College, Brunswick, ME 04011
dc.description.affiliationUnespDepartment of Biological Sciences School of Pharmacy São Paulo State University, Araraquara, SP, 14801-902
dc.format.extent393-405
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/11861547
dc.identifier.citationGenetics, v. 160, n. 2, p. 393-405, 2002.
dc.identifier.file2-s2.0-0036188448.pdf
dc.identifier.issn0016-6731
dc.identifier.lattes5333250355049814
dc.identifier.scopus2-s2.0-0036188448
dc.identifier.urihttp://hdl.handle.net/11449/66852
dc.identifier.wosWOS:000174097600006
dc.language.isoeng
dc.relation.ispartofGenetics
dc.relation.ispartofjcr4.075
dc.relation.ispartofsjr3,484
dc.rights.accessRightsAcesso abertopt
dc.sourceScopus
dc.subjectbinding protein
dc.subjectinitiation factor 5A
dc.subjectmessenger RNA
dc.subjectnuclear protein
dc.subjectprotein
dc.subjectprotein kinase C
dc.subjectallele
dc.subjectcell wall
dc.subjectgene interaction
dc.subjectgene mutation
dc.subjectgene overexpression
dc.subjecthigh temperature
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein degradation
dc.subjectprotein protein interaction
dc.subjectsignal transduction
dc.subjectstrain difference
dc.subjecttemperature sensitivity
dc.subjectyeast
dc.subjectAlleles
dc.subjectMutation, Missense
dc.subjectPeptide Initiation Factors
dc.subjectPoly(A)-Binding Proteins
dc.subjectProtein Kinase C
dc.subjectRNA-Binding Proteins
dc.subjectSaccharomyces cerevisiae
dc.subjectSignal Transduction
dc.subjectTemperature
dc.subjectEukaryota
dc.subjectFungi
dc.subjectMyxogastria
dc.subjectSaccharomyces
dc.titleGenetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signalingen
dc.typeArtigopt
dspace.entity.typePublication
relation.isDepartmentOfPublication5004bcab-94af-4939-b980-091ae9d0a19e
relation.isDepartmentOfPublication.latestForDiscovery5004bcab-94af-4939-b980-091ae9d0a19e
relation.isOrgUnitOfPublication95697b0b-8977-4af6-88d5-c29c80b5ee92
relation.isOrgUnitOfPublication.latestForDiscovery95697b0b-8977-4af6-88d5-c29c80b5ee92
unesp.author.lattes5333250355049814
unesp.author.orcid0000-0002-1098-9241[3]
unesp.campusUniversidade Estadual Paulista (UNESP), Faculdade de Ciências Farmacêuticas, Araraquarapt
unesp.departmentCiências Biológicas - FCFpt

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