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dc.contributor.authorValentini, Sandro Roberto [UNESP]
dc.contributor.authorWeiss, Valerie H.
dc.contributor.authorSilver, Pamela A.
dc.date.accessioned2014-05-27T11:19:42Z
dc.date.available2014-05-27T11:19:42Z
dc.date.issued1999-02-01
dc.identifierhttp://dx.doi.org/10.1017/S1355838299981633
dc.identifier.citationRNA, v. 5, n. 2, p. 272-280, 1999.
dc.identifier.issn1355-8382
dc.identifier.urihttp://hdl.handle.net/11449/65712
dc.description.abstractHrp1p is a heterogeneous ribonucleoprotein (hnRNP) from the yeast Saccharomyces cerevisiae that is involved in the cleavage and polyadenylation of the 3'-end of mRNAs and mRNA export. In addition, Hrp1p is one of several RNA-binding proteins that are posttranslationally modified by methylation at arginine residues. By using-functional recombinant Hrp1p, we have identified RNA sequences with specific high affinity binding sites. These sites correspond to the efficiency element for mRNA 3'-end formation, UAUAUA. To examine the effect of methylation on specific RNA binding, purified recombinant arginine methyltransferase (Hmt1p) was used to methylate Hrp1p. Methylated Hrp1p binds with the same affinity to UAUAUA-containing RNAs as unmethylated Hrp1p indicating that methylation does not affect specific RNA binding. However, RNA itself inhibits the methylation of Hrp1p and this inhibition is enhanced by RNAs that specifically bind Hrp1p. Taken together, these data support a model in which protein methylation occurs prior to protein-RNA binding in the nucleus.en
dc.format.extent272-280
dc.language.isoeng
dc.relation.ispartofRNA
dc.sourceScopus
dc.subjectCleavage
dc.subjectHmt1p
dc.subjecthnRNPs
dc.subjectPolyadenylation
dc.subjectRNA binding
dc.subjectarginine
dc.subjectmessenger RNA
dc.subjectmethyltransferase
dc.subjectribonucleoprotein
dc.subjectribonucleoprotein hrp1p
dc.subjectRNA binding protein
dc.subjectunclassified drug
dc.subjectbinding site
dc.subjectcell nucleus
dc.subjectcontrolled study
dc.subjectnonhuman
dc.subjectpolyadenylation
dc.subjectpriority journal
dc.subjectprotein methylation
dc.subjectprotein RNA binding
dc.subjectreverse transcription polymerase chain reaction
dc.subjectRNA cleavage
dc.subjectRNA processing
dc.subjectRNA sequence
dc.subjectsaccharomyces cerevisiae
dc.subjectAdenosine Triphosphatases
dc.subjectAmino Acid Sequence
dc.subjectArginine
dc.subjectBase Sequence
dc.subjectBinding Sites
dc.subjectCross-Linking Reagents
dc.subjectDNA Helicases
dc.subjectHeterogeneous-Nuclear Ribonucleoproteins
dc.subjectKinetics
dc.subjectMethylation
dc.subjectMethyltransferases
dc.subjectMolecular Sequence Data
dc.subjectOligoribonucleotides
dc.subjectProtein Binding
dc.subjectProtein Processing, Post-Translational
dc.subjectRecombinant Proteins
dc.subjectRibonucleoproteins
dc.subjectRNA, Messenger
dc.subjectRNA-Binding Proteins
dc.subjectSaccharomyces cerevisiae
dc.titleArginine methylation and binding of Hrp1p to the efficiency element for mRNA 3'-end formationen
dc.typeArtigo
dcterms.licensehttp://journals.cambridge.org/action/displaySpecialPage?pageId=4676
dc.contributor.institutionDana-Farber Cancer Institute
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.description.affiliationDept. Biol. Chem./Molec. Pharmacol. Harvard Medical School Dana-Farber Cancer Institute, Boston, MA 02115
dc.description.affiliationDana-Farber Cancer Institute, 44 Binney Street - SM922, Boston, MA 02115
dc.description.affiliationFaculdade de Cie. Farmaceuticas Univ. Estadual Paulista (UNESP), Araraquara, SP, 14801-902
dc.description.affiliationUnespFaculdade de Cie. Farmaceuticas Univ. Estadual Paulista (UNESP), Araraquara, SP, 14801-902
dc.identifier.doi10.1017/S1355838299981633
dc.rights.accessRightsAcesso restrito
dc.identifier.scopus2-s2.0-0033065488
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
dc.identifier.lattes5333250355049814
unesp.author.lattes5333250355049814
dc.relation.ispartofjcr4.490
dc.relation.ispartofsjr3,219
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