Plant Physiology Preview
Published on January 27, 2006; 10.1104/pp.105.073007
Received October 17, 2005
Returned for revision November 30, 2005
Accepted January 17, 2006
GOLD HULL AND INTERNODE2 (GH2) Encodes a Primarily Multifunctional Cinnamyl-Alcohol Dehydrogenase (CAD) in Oryza sativa
Kewei Zhang , Qian Qian , Zejun Huang , Yiqin Wang , Ming Li , Lilan Hong , Dali Zeng , Minghong Gu , Chengcai Chu , and Zhukuan Cheng *
State Key Laboratory of Plant Genomics and National Center for Plant Gene Research, Insitute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, P.R. China; Graduate School of the Chinese Academy of Sciences, Beijing, P.R. China
State Key Laboratory of Rice Biology, China National Rice Research Institute, Hangzhou 310006, P.R. China
State Key Laboratory of Plant Genomics and National Center for Plant Gene Research, Insitute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, P.R. China
State Key Laboratory of Plant Genomics and National Center for Plant Gene Research, Insitute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, P.R. China; State Key Laboratory of Rice Biology, China National Rice Research Institute, Hangzhou 310006, P.R. China; Graduate School of the Chinese Academy of Sciences, Beijing, P.R. China
Department of Agronomy, Yangzhou University, Yangzhou 225009, P.R. China
* Corresponding author; email: zkcheng{at}genetics.ac.cn.
Lignin content and composition are two important agronomic traits for the utilization of agricultural residues. Rice gold hull and internode phenotype is a classical morphological marker-trait that has long been applied to breeding and genetics study. In the present study, we have cloned GOLD HULL AND INTERNODE2 (GH2) gene in rice using a map-based cloning approach. The result shows that gh2 mutant is a lignin-deficient mutant, and GH2 encodes a cinnamyl-alcohol dehydrogenase (CAD). Consistent with this finding, extracts from roots, internodes, hulls and panicles of the gh2 plants exhibited drastically reduced CAD activity and undetectable sinapyl alcohol dehydrogenase (SAD) activity. When expressed in Escherichia coli (E. coli), purified recombinant GH2 was found to exhibit strong catalytic ability towards coniferaldehyde and sinapaldehyde, while the mutant protein gh2 completely lost the corresponding CAD and SAD activities. Further phenotypic analysis of the gh2 mutant plants revealed that the p-hydroxyphenyl, guaiacyl and sinapyl monomers were reduced in almost the same ratio compared to the wild type. Our results suggest GH2 acts as a primarily multifunctional CAD to synthesize coniferyl and sinapyl alcohol precursors in rice lignin biosynthesis.
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