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J. Biol. Chem., Vol. 277, Issue 26, 23447-23452, June 28, 2002
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From the 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 Ncyt-Ccyt (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.
Insertion and Topology of a Plant Viral Movement Protein in the
Endoplasmic Reticulum Membrane*
§,¶,
,,, and
Departament de Bioquímica i Biologia
Molecular, Universitat de València, E-46 100 Burjassot,
Spain, the Department of Biochemistry and Biophysics,
Stockholm University, SE-106 91 Stockholm, Sweden, and the
** Departamento de Ciencia de los Alimentos, Instituto de
Agroquímica y Tecnología de Alimentos, CSIC,
E-46 100 Burjassot, Spain
*
This work has been supported by Grant BMC2000-1448 from the
Spanish Ministerio de Ciencia y Tecnología (to I. M.), Grant BIO4-CT97-2086 from the European Union Biotechnology (to
E. P.-P.), and grants from the Swedish Cancer Foundation and the
Swedish Research Council (to G. v. H.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
34-96-386-4385; Fax: 34-96-386-4635; E-mail:
Ismael.Mingarro@uv.es.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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