Functional significance of eIF5A and its hypusine modification in eukaryotes

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dc.contributor.authorPark, M. H.
dc.contributor.authorNishimura, K.
dc.contributor.authorZanelli, Cleslei Fernando [UNESP]
dc.contributor.authorValentini, Sandro Roberto [UNESP]
dc.contributor.institutionNatl Inst Dent & Craniofacial Res
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:24:14Z
dc.date.available2014-05-20T13:24:14Z
dc.date.issued2010-02-01
dc.description.abstractThe unusual basic amino acid, hypusine [N(epsilon)-(4-amino-2-hydroxybutyl)-lysine], is a modified lysine with the addition of the 4-aminobutyl moiety from the polyamine spermidine. This naturally occurring amino acid is a product of a unique posttranslational modification that occurs in only one cellular protein, eukaryotic translation initiation factor 5A (eIF5A, eIF-5A). Hypusine is synthesized exclusively in this protein by two sequential enzymatic steps involving deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). The deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, and eIF5A, DHS and DOHH are highly conserved suggesting a vital cellular function of eIF5A. Gene disruption and mutation studies in yeast and higher eukaryotes have provided valuable information on the essential nature of eIF5A and the deoxyhypusine/hypusine modification in cell growth and in protein synthesis. In view of the extraordinary specificity and functional significance of hypusine-containing eIF5A in mammalian cell proliferation, eIF5A and the hypusine biosynthetic enzymes are novel potential targets for intervention in aberrant cell proliferation.en
dc.description.affiliationNatl Inst Dent & Craniofacial Res, Oral & Pharyngeal Canc Branch, NIH, Bethesda, MD 20892 USA
dc.description.affiliationSão Paulo State Univ, Sch Pharmaceut Sci, Dept Biol Sci, Araraquara, Brazil
dc.description.affiliationUnespSão Paulo State Univ, Sch Pharmaceut Sci, Dept Biol Sci, Araraquara, Brazil
dc.description.sponsorshipIntramural Research Program of National Institute of Dental and Craniofacial Research (NIDCR)
dc.description.sponsorshipNIH
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipKANAE Foundation
dc.format.extent491-500
dc.identifierhttp://dx.doi.org/10.1007/s00726-009-0408-7
dc.identifier.citationAmino Acids. New York: Springer, v. 38, n. 2, p. 491-500, 2010.
dc.identifier.doi10.1007/s00726-009-0408-7
dc.identifier.issn0939-4451
dc.identifier.lattes5333250355049814
dc.identifier.lattes1525665408900195
dc.identifier.orcid0000-0001-7831-1149
dc.identifier.urihttp://hdl.handle.net/11449/7456
dc.identifier.wosWOS:000274384100015
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofAmino Acids
dc.relation.ispartofjcr2.906
dc.relation.ispartofsjr1,135
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectHypusineen
dc.subjecteIF5Aen
dc.subjectPosttranslational modificationen
dc.subjectPolyamineen
dc.subjectDeoxyhypusine synthaseen
dc.subjectDeoxyhypusine hydroxylaseen
dc.subjectGene inactivationen
dc.titleFunctional significance of eIF5A and its hypusine modification in eukaryotesen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer
unesp.author.lattes5333250355049814
unesp.author.lattes1525665408900195[3]
unesp.author.orcid0000-0001-7831-1149[3]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt

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