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Insertion and topology of a plant viral movement protein in the Endoplasmic Reticulum membrane

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Insertion and topology of a plant viral movement protein in the Endoplasmic Reticulum membrane

dc.contributor.author	Vilar, Marçal
dc.contributor.author	Saurí Peris, Ana
dc.contributor.author	Monné, Magnus
dc.contributor.author	Marcos López, José Francisco
dc.contributor.author	Heijne, Gunnar von
dc.contributor.author	Pérez Payá, Enrique
dc.contributor.author	Mingarro Muñoz, Ismael
dc.date.accessioned	2016-09-08T14:39:02Z
dc.date.available	2016-09-08T14:39:02Z
dc.date.issued	2002
dc.identifier.citation	Vilar, Marçal Saurí Peris, Ana Monné, Magnus Marcos López, José Francisco Heijne, Gunnar von Pérez Payá, Enrique Mingarro Muñoz, Ismael 2002 Insertion and topology of a plant viral movement protein in the Endoplasmic Reticulum membrane Journal of Biological Chemistry 277 26 23447 23452
dc.identifier.uri	http://hdl.handle.net/10550/54969
dc.description.abstract	Virus-encoded movement proteins (MPs) mediate cell-to-cell spread of viral RNA through plant membranous intercellular connections, the plasmodesmata. The molecular pathway by which MPs interact with viral genomes and target plasmodesmata channels is largely unknown. The 9-kDa MP from carnation mottle carmovirus (CarMV) contains two potential transmembrane domains. To explore the possibility that this protein is in fact an intrinsic membrane protein, we have investigated its insertion into the endoplasmic reticulum membrane. By using in vitro translation in the presence of dog pancreas microsomes, we demonstrate that CarMV p9 inserts into the endoplasmic reticulum without the aid of any additional viral or plant host components. We further show that the membrane topology of CarMV p9 is N(cyt)-C(cyt) (N and C termini of the protein facing the cytoplasm) by in vitro translation of a series of truncated and full-length constructs with engineered glycosylation sites. Based on these results, we propose a topological model in which CarMV p9 is anchored in the membrane with its N- and C-terminal tail segments interacting with its soluble, RNA-bound partner CarMV p7, to accomplish the viral cell-to-cell movement function.
dc.language.iso	eng
dc.relation.ispartof	Journal of Biological Chemistry, 2002, vol. 277, num. 26, p. 23447-23452
dc.subject	Proteïnes de membrana
dc.subject	Virus
dc.subject	Bioquímica
dc.title	Insertion and topology of a plant viral movement protein in the Endoplasmic Reticulum membrane
dc.type	journal article	es_ES
dc.date.updated	2016-09-08T14:39:02Z
dc.identifier.doi	10.1074/jbc.M202935200
dc.identifier.idgrec	003981
dc.rights.accessRights	open access	es_ES