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RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins

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RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins

dc.contributor.author	Navarro Bohigues, José Antonio
dc.contributor.author	Genovés, A.
dc.contributor.author	Climent, J.
dc.contributor.author	Saurí Peris, Ana
dc.contributor.author	Martínez Gil, Luis
dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Pallás Benet, Vicente
dc.date.accessioned	2016-11-30T16:08:53Z
dc.date.available	2016-11-30T16:08:53Z
dc.date.issued	2006
dc.identifier.citation	Navarro Bohigues, José Antonio Genovés, A. Climent, J. Saurí Peris, Ana Martínez Gil, Luis Mingarro Muñoz, Ismael Pallás Benet, Vicente 2006 RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins Virology 356 1 57 67
dc.identifier.uri	http://hdl.handle.net/10550/56213
dc.description.abstract	Advances in structural and biochemical properties of carmovirus movement proteins (MPs) have only been obtained in p7 and p9 from Carnation mottle virus (CarMV). Alignment of carmovirus MPs revealed a low conservation of amino acid identity but interestingly, similarity was elevated in regions associated with the functional secondary structure elements reported for CarMV which were conserved in all studied proteins. Nevertheless, some differential features in relation with CarMV MPs were identified in those from Melon necrotic virus (MNSV) (p7A and p7B). p7A was a soluble non-sequence specific RNA-binding protein, but unlike CarMV p7, its central region alone could not account for the RNA-binding properties of the entire protein. In fact, a 22-amino acid synthetic peptide whose sequence corresponds to this central region rendered an apparent dissociation constant (K(d)) significantly higher than that of the corresponding entire protein (9 mM vs. 0.83-25.7 microM). This p7A-derived peptide could be induced to fold into an alpha-helical structure as demonstrated for other carmovirus p7-like proteins. Additionally, in vitro fractionation of p7B transcription/translation mixtures in the presence of ER-derived microsomal membranes strongly suggested that p7B is an integral membrane protein. Both characteristics of these two small MPs forming the double gene block (DGB) of MNSV are discussed in the context of the intra- and intercellular movement of carmovirus.
dc.language.iso	eng
dc.relation.ispartof	Virology, 2006, vol. 356, num. 1, p. 57-67
dc.subject	Proteïnes de membrana
dc.subject	Membranes (Biologia)
dc.subject	Virus
dc.title	RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins
dc.type	journal article	es_ES
dc.date.updated	2016-11-30T16:08:53Z
dc.identifier.doi	10.1016/j.virol.2006.07.040
dc.identifier.idgrec	033788
dc.rights.accessRights	open access	es_ES