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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleThe acidic domain of hnRNPQ (NSAP1) has structural similarity to Barstar and binds to Apobec1pt_BR
dc.contributor.authorQuaresma, AJCpt_BR
dc.contributor.authorOyama, Spt_BR
dc.contributor.authorBarbosa, JARGpt_BR
dc.contributor.authorKobarg, Jpt_BR
unicamp.author.emailjkobarg@lnls.brpt_BR
unicamp.authorLab Nacl Luz Sincrotron, Ctr Biol Mol Estruct, BR-13084971 Campinas, SP, Brazil Univ Estadual Campinas, Dept Bioquim, BR-13084970 Campinas, SP, Brazil Univ Estadual Campinas, Dept Genet & Evolucao, BR-13084970 Campinas, SP, Brazilpt_BR
dc.subjecthnRNPQ/NSAP1pt_BR
dc.subjectApobec1pt_BR
dc.subjectAcD domainpt_BR
dc.subjectRNA editingpt_BR
dc.subjectmolecular modelingpt_BR
dc.subjectmolecular dynamicspt_BR
dc.subjectprotein-protein interactionspt_BR
dc.subjectcircular dichroismpt_BR
dc.subject.wosB Messenger-rnapt_BR
dc.subject.wosComplementation Factorpt_BR
dc.subject.wosCytidine Deaminasept_BR
dc.subject.wosEditing Proteinpt_BR
dc.subject.wosInteractspt_BR
dc.subject.wosSequencept_BR
dc.subject.wosPhosphorylationpt_BR
dc.subject.wosIdentificationpt_BR
dc.subject.wosRecognitionpt_BR
dc.subject.wosComplexpt_BR
dc.description.abstractApobecl edits the ApoB mRNA by deaminating nucleotide C-6666, which results in a codon change from Glutamate to stop, and subsequent expression of a truncated protein. Apobecl is regulated by ACF (Apobecl complementation factor) and hnRNPQ, which contains an N-terminal 'acidic domain' (AcD) of unknown function, three RNA recognition motifs, and an Arg/Gly-rich region. Here, we modeled the structure of AcD using the bacterial protein Barstar as a template. Furthermore, we demonstrated by in vitro pull-down assays that 6xHis-AcD alone is able to interact with GST-Apobecl. Finally, we performed in silico phosphorylation of AcD and molecular dynamics studies, which indicate conformational changes in the phosphorylated form. The results of the latter studies were confirmed by in vitro phosphorylation of 6xHis-AcD by protein kinase C, mass spectrometry, and spectroscopic analyses. Our data suggest hnRNPQ interactions via its AcD with Apobecl and that this interaction is regulated by the AcD phosphorylation. (c) 2006 Elsevier Inc. All rights reserved.pt
dc.relation.ispartofBiochemical And Biophysical Research Communicationspt_BR
dc.relation.ispartofabbreviationBiochem. Biophys. Res. Commun.pt_BR
dc.publisher.citySan Diegopt_BR
dc.publisher.countryEUApt_BR
dc.publisherAcademic Press Inc Elsevier Sciencept_BR
dc.date.issued2006pt_BR
dc.date.monthofcirculation43040pt_BR
dc.identifier.citationBiochemical And Biophysical Research Communications. Academic Press Inc Elsevier Science, v. 350, n. 2, n. 288, n. 297, 2006.pt_BR
dc.language.isoenpt_BR
dc.description.volume350pt_BR
dc.description.issuenumber2pt_BR
dc.description.firstpage288pt_BR
dc.description.lastpage297pt_BR
dc.rightsfechadopt_BR
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policypt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn0006-291Xpt_BR
dc.identifier.wosidWOS:000241389900006pt_BR
dc.identifier.doi10.1016/j.bbrc.2006.09.044pt_BR
dc.date.available2014-11-15T08:02:06Z
dc.date.available2015-11-26T16:10:09Z-
dc.date.accessioned2014-11-15T08:02:06Z
dc.date.accessioned2015-11-26T16:10:09Z-
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dc.description.provenanceMade available in DSpace on 2015-11-26T16:10:09Z (GMT). No. of bitstreams: 2 WOS000241389900006.pdf: 1809535 bytes, checksum: 934420669334552eb7e24c31437bbd7f (MD5) WOS000241389900006.pdf.txt: 44814 bytes, checksum: dedc8a88084ad7833cb99e51cba15ca5 (MD5) Previous issue date: 2006en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/78688pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/78688
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/78688-
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