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Published on October 30, 2009; 10.1104/pp.109.145078

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Received July 22, 2009
Accepted October 27, 2009

MODIFIED VACUOLE PHENOTYPE1 Is an Arabidopsis Myrosinase-Associated Protein Involved in Endomembrane Protein Trafficking

April E. Agee , Marci Surpin , Eun Ju Sohn , Thomas Girke , Abel Rosado , Brian W. Kram , Clay Carter , Adam M. Wentzell , Daniel J. Kliebenstein , Hak Chul Jin , Ohkmae K. Park , Hailing Jin , Glenn R. Hicks , and Natasha Raikhel *

Department of Botany and Plant Sciences and Center for Plant Cell Biology, University of California, Riverside, Riverside, CA 92521; Department of Biology, University of Minnesota Duluth, 207 SSB, 1035 Kirby Dr., Duluth, MN 55812; Genetics Graduate Group and Department of Plant Sciences, University of California, Davis, Davis, California 95616; School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea; Department of Plant Pathology and Microbiology and Center for Plant Cell Biology, University of California, Riverside, Riverside, CA 92521; Institute for Integrative Genome Biology, University of California, Riverside, Riverside, CA 92521

* Corresponding author; email: natasha.raikhel{at}ucr.edu.

We identified an Arabidopsis thaliana EMS mutant, modified vacuole phenotype1-1 (mvp1-1), in a fluorescent confocal microscopy screen for plants with mislocalization of a GFP-{delta} tonoplast intrinsic protein fusion. The mvp1-1 mutant displayed static perinuclear aggregates of the reporter protein. mvp1 mutants also exhibited a number of vacuole-related phenotypes, as demonstrated by defects in growth, utilization of stored carbon, gravitropic response, salt sensitivity and specific susceptibility to the fungal necrotroph Alternaria brassicicola. Similarly, crosses with other endomembrane marker fusions identified mislocalization to aggregate structures, indicating a general defect in protein trafficking. Map-based cloning showed that the mvp1-1 mutation altered a gene encoding a putative myrosinase-associated protein, and GST-pulldown assays demonstrated that MVP1 interacted specifically with the Arabidopsis myrosinase protein, TGG2, but not TGG1. Moreover, the mvp1-1 mutant showed increased nitrile production during glucosinolate hydrolysis, suggesting that MVP1 may play a role in modulation of myrosinase activity. We propose that MVP1 is a myrosinase-associated protein that functions, in part, to correctly localize the myrosinase TGG2 and prevent inappropriate glucosinolate hydrolysis that could generate cytotoxic molecules.






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