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First published online September 17, 2004; 10.1105/tpc.104.025171

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The Plant Cell 16:2795-2808 (2004)
© 2004 American Society of Plant Biologists

Spotted leaf11, a Negative Regulator of Plant Cell Death and Defense, Encodes a U-Box/Armadillo Repeat Protein Endowed with E3 Ubiquitin Ligase Activity{boxw}

Li-Rong Zenga, Shaohong Qua, Alicia Bordeosb, Chengwei Yangc, Marietta Baraoidanb, Hongyan Yanc, Qi Xiec, Baek Hie Nahmd, Hei Leungb and Guo-Liang Wanga,1

a Department of Plant Pathology, Ohio State University, Columbus, Ohio 43210
b International Rice Research Institute, Metro Manila, Philippines
c State Key Lab for Biocontrol, Sun Yat-sen (Zhongshan) University, Guangzhou, China 510275
d Department of Biological Science, Myongji University, Kyonggido, Korea 449728

1 To whom correspondence should be addressed. E-mail wang.620{at}osu.edu; fax 614-292-4455.

The rice (Oryza sativa) spotted leaf11 (spl11) mutant was identified from an ethyl methanesulfonate–mutagenized indica cultivar IR68 population and was previously shown to display a spontaneous cell death phenotype and enhanced resistance to rice fungal and bacterial pathogens. Here, we have isolated Spl11 via a map-based cloning strategy. The isolation of the Spl11 gene was facilitated by the identification of three additional spl11 alleles from an IR64 mutant collection. The predicted SPL11 protein contains both a U-box domain and an armadillo (ARM) repeat domain, which were demonstrated in yeast and mammalian systems to be involved in ubiquitination and protein–protein interactions, respectively. Amino acid sequence comparison indicated that the similarity between SPL11 and other plant U-box-ARM proteins is mostly restricted to the U-box and ARM repeat regions. A single base substitution was detected in spl11, which results in a premature stop codon in the SPL11 protein. Expression analysis indicated that Spl11 is induced in both incompatible and compatible rice–blast interactions. In vitro ubiquitination assay indicated that the SPL11 protein possesses E3 ubiquitin ligase activity that is dependent on an intact U-box domain, suggesting a role of the ubiquitination system in the control of plant cell death and defense.




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