dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorGregio, Ana P. B.
dc.creatorCano, Veridiana P. S.
dc.creatorAvaca, Juliana S.
dc.creatorValentini, Sandro Roberto
dc.creatorZanelli, Cleslei Fernando
dc.date2014-05-20T13:24:15Z
dc.date2016-10-25T16:44:59Z
dc.date2014-05-20T13:24:15Z
dc.date2016-10-25T16:44:59Z
dc.date2009-03-20
dc.date.accessioned2017-04-05T19:59:33Z
dc.date.available2017-04-05T19:59:33Z
dc.identifierBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 380, n. 4, p. 785-790, 2009.
dc.identifier0006-291X
dc.identifierhttp://hdl.handle.net/11449/7475
dc.identifierhttp://acervodigital.unesp.br/handle/11449/7475
dc.identifier10.1016/j.bbrc.2009.01.148
dc.identifierWOS:000264271100013
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2009.01.148
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/856108
dc.descriptionThe putative translation factor eIF5A is essential for cell viability and is highly conserved throughout evolution. Here, we describe genetic interactions between an eIF5A Mutant and a translation initiation mutant (eIF4E) or a translation elongation mutant (eEF2). Polysome profile analysis of single and double mutants revealed that mutation in eIF5A reduces polysome run-off, contrarily to translation initiation mutants. Moreover, the polysome profile of an eIF5A mutant alone is very similar to that of a translation elongation mutant. Furthermore, depletion of eIF5A causes a significant decrease in total protein synthesis and an increase of the average ribosome transit time. Finally, we, demonstrate that the formation of P bodies is inhibited in an eIF5A mutant, similarly to the effect of the translation elongation inhibitor cycloheximide. taken together, these results not only reinforce a role for eIF5A in translation but also strongly support a function for eIF5A in the elongation step of protein synthesis. (C) 2009 Elsevier B.V. All rights reserved.
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageeng
dc.publisherAcademic Press Inc. Elsevier B.V.
dc.relationBiochemical and Biophysical Research Communications
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjecteIF5A
dc.subjectTranslation elongation
dc.subjecteEF2
dc.subjectRibosome transit time
dc.subjectEF-P
dc.subjectHypusine
dc.titleeIF5A has a function in the elongation step of translation in yeast
dc.typeOtro


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