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Published on August 22, 2008; 10.1104/pp.108.123547

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Received May 26, 2008
Accepted August 11, 2008

Abnormal chloroplast development and growth inhibition in Oryza sativa thioredoxin m knock-down plants

Yong Hun Chi , Jeong Chan Moon , Jin Ho Park , Ho-Seung Kim , Ismayil S. Zulfugarov , Wahyu Indra Fanata , Ho Hee Jang , Jung Ro Lee , Young Mee Lee , Sun Tae Kim , Yong-Yoon Chung , Chae Oh Lim , Jae-Yean Kim , Dae-Jin Yun , Choon-Hwan Lee , Kyun Oh Lee *, and Sang Yeol Lee

Division of Applied Life Science (BK21 Program), EB-NCRC and PMBBRC, Gyeongsang National University, 900 Gajwa-dong, Jinju 660-701, Korea; Department of Molecular Biology, Pusan National University, Busan 609-735, Korea; School of Life Sciences and Biotechnology, Korea University, Korea

* Corresponding author; email: leeko{at}gnu.ac.kr.

Plant cells contain several thioredoxin isoforms which are characterized by subcellular localization and substrate specificity. Here we describe the functional characterization of an Oryza sativa thioredoxin m isoform (Ostrxm) using a reverse genetics technique. Ostrxm showed green tissue-specific and light-responsive mRNA expression. Ostrxm was localized in chloroplasts of rice mesophyll cells, and the recombinant protein showed DTT-dependent insulin {beta}-chain reduction activity in vitro. RNA interference (RNAi) of Ostrxm resulted in rice plants with developmental defects including semi-dwarfism, pale green leaves, abnormal chloroplast structure, and reduced carotenoid and chlorophyll contents. Ostrxm RNAi plants showed remarkably decreased Fv/Fm values under high irradiance conditions (1,000 µmol m-2 s-1) with delayed recovery. Two-dimensional electrophoresis and MALDI-TOF analysis showed that the levels of several chloroplast proteins critical for photosynthesis and biogenesis were significantly decreased in Ostrxm RNAi plants. Furthermore, 2-Cys peroxiredoxin (2-Cys Prx), a known target of thioredoxin, was present in oxidized forms, and hydrogen peroxide levels were increased in Ostrxm RNAi plants. The pleiotropic effects of Ostrxm RNAi suggest that Ostrxm plays an important role in the redox regulation of chloroplast target proteins involved in diverse physiological functions.






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