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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleDeletion mapping of the potyviral helper component-proteinase reveals two regions involved in RNA bindingpt_BR
dc.contributor.authorUrcuqui-Inchima, Spt_BR
dc.contributor.authorMaia, IGpt_BR
dc.contributor.authorArruda, Ppt_BR
dc.contributor.authorHaenni, ALpt_BR
dc.contributor.authorBernardi, Fpt_BR
unicamp.authorInst Jacques Monod, F-75251 Paris 05, France UNICAMP, Ctr Biol Mol & Engn Genet, Campinas, SP, Brazil Univ Paris Sud, Inst Biotechnol Plantes, F-91405 Orsay, Francept_BR
dc.subject.wosTobacco Etch Potyviruspt_BR
dc.subject.wosHc-propt_BR
dc.subject.wosGenome Amplificationpt_BR
dc.subject.wosSecondary Structurept_BR
dc.subject.wosCentral Domainpt_BR
dc.subject.wosPlant-virusespt_BR
dc.subject.wosGenept_BR
dc.subject.wosMutationspt_BR
dc.subject.wosSequencept_BR
dc.subject.wosTransmissionpt_BR
dc.description.abstractThe Potyvirus helper component-proteinase (HC-Pro) binds nonspecifically to single-stranded nucleic acids with a preference for RNA To delineate the regions of the protein responsible for RNA binding, deletions were introduced into the full-length Potato potyvirus Y HC-Pro gene carried by an Escherichia coil expression vector. The corresponding proteins were expressed as fusions with the maltose-binding protein, purified, and assayed for their RNA-binding capacity. The results obtained by UV cross-linking and Northwestern blot assays demonstrated that the N- and C-terminal regions of HC-Pro are dispensable for RNA binding. They also revealed the presence of two independent RNA-binding domains (designated A and B) located in the central part of HC-Pro. Domain B appears to contain a ribonucleoprotein (RNP) motif typical of a large family of RNA-binding proteins involved in several cellular processes. The possibility that domain a consists of an RNP domain is discussed and suggests that HC-Pro could constitute the first example of a plant viral protein belonging to the RNP-containing family of proteins. (C) 2000 Academic Press.pt
dc.relation.ispartofVirologypt_BR
dc.relation.ispartofabbreviationVirologypt_BR
dc.publisher.citySan Diegopt_BR
dc.publisher.countryEUApt_BR
dc.publisherAcademic Press Incpt_BR
dc.date.issued2000pt_BR
dc.date.monthofcirculation36951pt_BR
dc.identifier.citationVirology. Academic Press Inc, v. 268, n. 1, n. 104, n. 111, 2000.pt_BR
dc.language.isoenpt_BR
dc.description.volume268pt_BR
dc.description.issuenumber1pt_BR
dc.description.firstpage104pt_BR
dc.description.lastpage111pt_BR
dc.rightsfechadopt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn0042-6822pt_BR
dc.identifier.wosidWOS:000085797200013pt_BR
dc.identifier.doi10.1006/viro.1999.0156pt_BR
dc.date.available2014-12-02T16:29:16Z
dc.date.available2015-11-26T16:38:56Z-
dc.date.accessioned2014-12-02T16:29:16Z
dc.date.accessioned2015-11-26T16:38:56Z-
dc.description.provenanceMade available in DSpace on 2014-12-02T16:29:16Z (GMT). No. of bitstreams: 1 WOS000085797200013.pdf: 224373 bytes, checksum: ea935f633faa57474253008f9d36bc84 (MD5) Previous issue date: 2000en
dc.description.provenanceMade available in DSpace on 2015-11-26T16:38:56Z (GMT). No. of bitstreams: 2 WOS000085797200013.pdf: 224373 bytes, checksum: ea935f633faa57474253008f9d36bc84 (MD5) WOS000085797200013.pdf.txt: 36599 bytes, checksum: 877ab0afa12c4a707f289fdf49684b02 (MD5) Previous issue date: 2000en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/79427pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/79427
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/79427-
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