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BREAKTHROUGH TECHNOLOGIES

Coordinate Expression and Independent Subcellular Targeting of Multiple Proteins from a Single Transgene¹

Plant Research Unit, School of Life Sciences, University of Dundee (A.E.A., A.B., B.M.A., X.L., C.H.) and Cell Biology Group (A.G.R.), Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, Scotland, United Kingdom; and Division of Biomedical Science, School of Biology, University of St. Andrews, Fife KY16 9ST, Scotland, United Kingdom (M.D.R.)

A variety of conventional methods allow the expression of multiple foreign proteins in plants by transgene stacking or pyramiding. However, most of these approaches have significant drawbacks. We describe a novel alternative, using a single transgene to coordinate expression of multiple proteins that are encoded as a polyprotein capable of dissociating into component proteins on translation. We demonstrate that this polyprotein system is compatible with the need to target proteins to a variety of subcellular locations, either cotranslationally or posttranslationally. It can also be used to coordinate the expression of selectable marker genes and effect genes or to link genes that are difficult to assay to reporter genes that are easily monitored. The unique features of this polyprotein system are based on the novel activity of the 2A peptide of Foot-and-mouth disease virus (FMDV) that acts cotranslationally to effect a dissociation of the polyprotein while allowing translation to continue. This polyprotein system has many applications both as a research tool and for metabolic engineering and protein factory applications of plant biotechnology.

² These authors contributed equally to the paper.

³ Present address: Université de Rennes 1, Centre National de la Recherche Scientifique-Unité Mixte de Recherche 6553, Campus de Beaulieu, Bâtiment 14 A, 35042 Rennes cedex, France.

www.plantphysiol.org/cgi/doi/10.1104/pp.103.032649.

^* Corresponding author; e-mail c.halpin{at}dundee.ac.uk; fax 44–0–1382–568581.

Received September 2, 2003; returned for revision October 3, 2003; accepted February 10, 2004.

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