Cleavage of Arabidopsis PBS1 by a Bacterial Type III Effector

American Association for the Advancement of Science (AAAS) - Tập 301 Số 5637 - Trang 1230-1233 - 2003
Feng Shao1, Catherine Golstein1, Jules Ade1, Mark Stoutemyer1, Jack E. Dixon1, Roger W. Innes1
1Department of Biological Chemistry, Medical School and Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA. Department of Biology, Indiana University, Bloomington, IN 47405, USA.

Tóm tắt

Plant disease-resistance (R) proteins are thought to function as receptors for ligands produced directly or indirectly by pathogen avirulence (Avr) proteins. The biochemical functions of most Avr proteins are unknown, and the mechanisms by which they activate R proteins have not been determined. In Arabidopsis , resistance to Pseudomonas syringae strains expressing AvrPphB requires RPS5, a member of the class of R proteins that have a predicted nucleotide-binding site and leucine-rich repeats, and PBS1, a protein kinase. AvrPphB was found to proteolytically cleave PBS1, and this cleavage was required for RPS5-mediated resistance, which indicates that AvrPphB is detected indirectly via its enzymatic activity.

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Arabidopsis mutant alleles used in this work have been described previously ( 13 14 17 ). The pbs1-1 and rar1-20 mutations are protein null whereas rps5-2 and pbs1-2 are missense mutations that display complete loss-of-function phenotypes.

We thank Z. Bao and R. Kruger for technical assistance; M. Swiderski for the construction of a PBS1-HA plasmid; and P. Merritt M. Estelle and B. Staskawicz for comments on the manuscript. F.S. was supported by the Anthony and Lillian Lu graduate student fellowship. This work was supported by National Institutes of Health grants DK18849 (J.E.D.) and GM46451 (R.W.I.) the Walther Cancer Institute (J.E.D.) and the Ellison Medical Foundation (J.E.D.).

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American Association for the Advancement of Science (AAAS)

Tập 301 Số 5637

1230-1233

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