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First published online October 2, 2003; 10.1104/pp.103.025999

Plant Physiology 133:1072-1082 (2003)
© 2003 American Society of Plant Biologists

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PLANTS INTERACTING WITH OTHER ORGANISMS

Cleavage of the Pseudomonas syringae Type III Effector AvrRpt2 Requires a Host Factor(s) Common among Eukaryotes and Is Important for AvrRpt2 Localization in the Host Cell

Ping Jin1,2, Michelle D. Wood1,3, Yan Wu, Zhiyi Xie4 and Fumiaki Katagiri5,*

Torrey Mesa Research Institute,6, Syngenta Research and Technology, 3115 Merryfield Row, San Diego, California 92121 (P.J., M.D.W., Y.W., Z.X., F.K.); and Department of Biological Sciences, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, Maryland 21250 (M.D.W.)

Many phytopathogenic bacteria use a type III secretion system to deliver type III effector proteins into the host plant cell. The Pseudomonas syringae type III effector AvrRpt2 is cleaved at a specific site when translocated into the host cell. In this study, we first demonstrate that the factor(s) required for AvrRpt2 cleavage is present in extracts from animal and yeast cells, as well as plant cells. The cleavage factor in animal and plant cell extracts was heat labile but relatively insensitive to protease inhibitors. Second, mutational analysis of AvrRpt2 was applied to identify features important for its cleavage. In addition to two of the amino acid residues in the immediate vicinity of the cleavage site, a large part of the region C-terminal to the cleavage site was required when AvrRpt2 was cleaved in animal cell extract. Most of these features were also important when AvrRpt2 was cleaved in plant cells. Third, we investigated the effect of cleavage in interactions of AvrRpt2 with plant cells. Cleavage of AvrRpt2 appeared to be important for proper interactions with Arabidopsis cells that lack the resistance gene product corresponding to AvrRpt2, RPS2. In addition, removal of the region N-terminal to the cleavage site was important for the correct localization of the C-terminal effector region of the protein in the host cell. We speculate that the virulence function of AvrRpt2 requires removal of the N-terminal region to redirect the effector protein to a specific subcellular location in the host cell after translocation of the protein.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.025999.

1 These authors contributed equally to this paper.

2 Present address: Diversa Corp., 4955 Directors Place, San Diego, CA 92121.

3 Present address: 9939 Azuaga Street H104, San Diego, CA 92129.

4 Present address: Biocept, Inc., 2151 Las Palmas Drive, Carlsbad, CA 92009.

5 Present address: Department of Plant Biology, University of Minnesota, 1445 Gortner Avenue, St. Paul, MN 55108.

6 Torrey Mesa Research Institute has been closed.

* Corresponding author; e-mail katagiri{at}umn.edu; fax 612–625–1738.

Received April 24, 2003; returned for revision June 1, 2003; accepted August 4, 2003.




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