Plant Physiology Preview
Published on August 1, 2002; 10.1104/pp.004754
Received February 23, 2002
Accepted March 27, 2002
A Novel Plant Homeodomain Protein Interacts in a Functionally Relevant Manner with a Virus Movement Protein
Bénédicte Desvoyes , Sandrine Faure-Rabasse , Min-Huei Chen , Jong-Won Park , and Herman B. Scholthof *
Department of Plant Pathology and Microbiology (B.D., S.F.-R., J.-W.P., H.B.S.) and Intercollegiate Faculty of Virology (H.B.S.), Texas A&M University, 2132 TAMU, College Station, Texas 77843; and Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, New York 11794--5215 (M.-H.C.)
* Corresponding author; email: herscho{at}tamu.edu.
Tomato bushy stunt virus and its cell-to-cell movement protein (MP; P22) provide valuable tools to study trafficking of macromolecules through plants. This study shows that wild-type P22 and selected movement-defective P22 amino acid substitution mutants were equivalent for biochemical features commonly associated with MPs (i.e. RNA binding, phosphorylation, and membrane partitioning). This generated the hypothesis that their movement defect was caused by improper interaction between the P22 mutants and one or more host factors. To test this, P22 was used as bait in a yeast (Saccharomyces cerevisiae) two-hybrid screen with a tobacco (Nicotiana tabacum) cDNA library, which identified a new plant homeodomain leucine-zipper protein that reproducibly interacted with P22 but not with various control proteins. These results were confirmed with an independent in vitro binding test. An mRNA for the host protein was detected in plants, and its accumulation was enhanced upon Tomato bushy stunt virus infection of two plant species. The significance of this interaction was further demonstrated by the failure of the homeodomain protein to interact efficiently with two of the well-defined movement-deficient P22 mutants in yeast and in vitro. This is the first report, to our knowledge, that a new plant homeodomain leucine-zipper protein interacts specifically and in a functionally relevant manner with a plant virus MP.
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