Synthetic lethality between eIF5A and Ypt1 reveals a connection between translation and the secretory pathway in yeast

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dc.contributor.authorFrigieri, Mariana C. [UNESP]
dc.contributor.authorLuiz, Marcus V. S. Joao [UNESP]
dc.contributor.authorApponi, Luciano H. [UNESP]
dc.contributor.authorZanelli, Cleslei Fernando [UNESP]
dc.contributor.authorValentini, Sandro Roberto [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:24:12Z
dc.date.available2014-05-20T13:24:12Z
dc.date.issued2008-09-01
dc.description.abstractThe putative translation initiation factor 5A (eIF5A) is a small protein, highly conserved and essential in all organisms from archaea to mammals. Although the involvement of eIF5A in translation initiation has been questioned, new evidence reestablished the connection between eIF5A and this cellular process. In order to better understand the function of elF5A, a screen for synthetic lethal gene using the tif51A-3 mutant was carried out and a new mutation (G80D) was found in the essential gene YPT1, encoding a protein involved in vesicular trafficking. The precursor form of the vacuolar protein CPY is accumulated in the ypt1-G80D mutant at the nonpermissive temperature, but this defect in vesicular trafficking did not occur in the tif51A mutants tested. Overexpression of eIF5A suppresses the growth defect of a series of ypt1 mutants, but this suppression does not restore correct CPY sorting. on the other hand, overexpression of YPT1 does not suppress the growth defect of tif51A mutants. Further, it was revealed that eIF-5A is present in both soluble and membrane fractions, and its membrane association is ribosome-dependent. Finally, we demonstrated that the ypt1 and other secretion pathway mutants are sensitive to paromomycin. These results confirm the link between translation and vesicular trafficking and reinforce the implication of eIF5A in protein synthesis.en
dc.description.affiliationUNESP, Sch Pharmaceut Sci, Dept Biol Sci, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUnespUNESP, Sch Pharmaceut Sci, Dept Biol Sci, BR-14801902 Araraquara, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipPrograma de Apoio ao Desenvolvimento Científico da Faculdade de Ciências Farmacêuticas da UNESP (PADC)
dc.format.extent211-221
dc.identifierhttp://dx.doi.org/10.1007/s00438-008-0357-y
dc.identifier.citationMolecular Genetics and Genomics. Heidelberg: Springer Heidelberg, v. 280, n. 3, p. 211-221, 2008.
dc.identifier.doi10.1007/s00438-008-0357-y
dc.identifier.issn1617-4615
dc.identifier.lattes5333250355049814
dc.identifier.lattes1525665408900195
dc.identifier.orcid0000-0001-7831-1149
dc.identifier.urihttp://hdl.handle.net/11449/7440
dc.identifier.wosWOS:000258540900003
dc.language.isoeng
dc.publisherSpringer Heidelberg
dc.relation.ispartofMolecular Genetics and Genomics
dc.relation.ispartofjcr2.734
dc.relation.ispartofsjr1,168
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjecteIF5Aen
dc.subjectYpt1en
dc.subjectsynthetic lethalityen
dc.subjectgenetic interactionen
dc.subjectvesicular traffickingen
dc.subjectprotein synthesisen
dc.titleSynthetic lethality between eIF5A and Ypt1 reveals a connection between translation and the secretory pathway in yeasten
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer Heidelberg
unesp.author.lattes5333250355049814
unesp.author.lattes1525665408900195[4]
unesp.author.orcid0000-0001-7831-1149[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt

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