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Plant Cell Advance Online Publication
Published on September 17, 2004; 10.1105/tpc.104.025171

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Received June 15, 2004
Accepted August 9, 2004

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

Li-Rong Zeng 1, Shaohong Qu 1, Alicia Bordeos 2, Chengwei Yang 3, Marietta Baraoidan 2, Hongyan Yan 3, Qi Xie 3, Baek Hie Nahm 4, Hei Leung 2, and Guo-Liang Wang 1*

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

* To whom correspondence should be addressed. E-mail: wang.620{at}osu.edu.

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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