Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D)

dc.creatorMoraes, KCM
dc.creatorQuaresma, AJC
dc.creatorMaehnss, K
dc.creatorKobarg, J
dc.date2003
dc.dateJAN
dc.date2014-11-14T23:30:55Z
dc.date2015-11-26T16:09:01Z
dc.date2014-11-14T23:30:55Z
dc.date2015-11-26T16:09:01Z
dc.date.accessioned2018-03-28T22:57:37Z
dc.date.available2018-03-28T22:57:37Z
dc.identifierBiological Chemistry. Walter De Gruyter & Co, v. 384, n. 1, n. 25, n. 37, 2003.
dc.identifier1431-6730
dc.identifierWOS:000180634700004
dc.identifier10.1515/BC.2003.004
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/69112
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/69112
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/69112
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1266514
dc.descriptionThe mRNAs that encode certain cytokines and protooncogenes frequently contain a typical AU-rich motif that is located in their 3'-untranslated region. The protein AUF1 is the first factor identified that binds to AU-rich regions and mediates the fast degradation of the target mRNAs. AUF1 exists as four different isoforms (p37, p40, p42 and p45) that are generated by alternative splicing. The fact that AUF1 does not degrade mRNA itself had led to the suggestion that other AUF1 interacting proteins might be involved in the process of selective mRNA degradation. Here we used the yeast twohybrid system in order to identify proteins that bind to AUF1. We detected AUF1 itself, as well as the ubiquitinconjugating enzyme E2I and three RNA binding proteins: NSEP-1, NSAP-1 and IMP-2, as AUF1 interacting proteins. We confirmed all interactions in vitro and mapped the protein domains that are involved in the interaction with AUF1. Gelshift assays with the recombinant purified proteins suggest that the interacting proteins and AUF1 can bind simultaneously to an AU-rich RNA oligonucleotide. Most interestingly, the AUF1 interacting protein NSEP-1showed an endoribonuclease activity in vitro. These data suggest the possibility that the identified AUF1 interacting proteins might be involved in the regulation of mRNA stability mediated by AUF1.
dc.descriptiono TEXTO COMPLETO DESTE ARTIGO, ESTARÁ DISPONÍVEL À PARTIR DE AGOSTO DE 2015.
dc.description384
dc.description1
dc.description25
dc.description37
dc.languageen
dc.publisherWalter De Gruyter & Co
dc.publisherBerlin
dc.publisherAlemanha
dc.relationBiological Chemistry
dc.relationBiol. Chem.
dc.rightsembargo
dc.sourceWeb of Science
dc.subjectdomain mapping
dc.subjectmRNA degradation
dc.subjectprotein-protein interactions
dc.subjectribonuclease
dc.subjectRNA binding domains
dc.subjectRNA binding proteins
dc.subjectMessenger-rna Stability
dc.subjectCold Shock Domain
dc.subject2-hybrid System
dc.subjectMammalian-cells
dc.subjectRich Elements
dc.subjectGene
dc.subjectTranscription
dc.subjectDeterminant
dc.subjectTranslation
dc.subjectInvitro
dc.titleIdentification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D)
dc.typeArtículos de revistas


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