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Published on April 1, 2009; 10.1104/pp.109.135426

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Received January 8, 2009
Accepted March 26, 2009

Heat-shock and redox-dependent functional switching of an h-type Arabidopsis thioredoxin from a disulfide reductase to a molecular chaperone

Soo Kwon Park , Young Jun Jung , Jung Ro Lee , Young Mee Lee , Ho Hee Jang , Seung Sik Lee , Jin Ho Park , Sun Young Kim , Jeong Chan Moon , Sun Yong Lee , Ho Byoung Chae , Mi Rim Shin , Ji Hyun Jung , Min Gab Kim , Woe Yeon Kim , Dae-Jin Yun , Kyun Oh Lee , and Sang Yeol Lee *

Environmental Biotechnology National Core Research Center, PMBBRC; Division of Applied Life Science (BK21 program), Gyeongsang National University, Jinju, 660-701, Korea; Lee Gil Ya Cancer & Diabetes Ins. Gacheon Univ. Medicine & Science, Korea; Department of Functional Crop, National Institute of Crop Science, Rural Development Administration, 627-130, Milyang, Korea; Bio-crops development Division, National Academy of Agricultural Science, RDA. 224 Suin-ro, Suwon 441-857, Korea

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

A large number of thioredoxins (Trxs), small redox proteins, have been identified from all living organisms. However, many of the physiological roles played by these proteins remain to be elucidated. We isolated a high molecular weight (HMW) form of h-type Trx from the heat-treated cytosolic extracts of Arabidopsis suspension cells and designated it as AtTrx-h3. Using bacterially expressed recombinant AtTrx-h3, we find that it forms various protein structures ranging from low and oligomeric protein species to HMW complexes. And the AtTrx-h3 performs dual functions, acting as a disulfide reductase and as a molecular chaperone, which are closely associated with its molecular structures. The disulfide reductase function is observed predominantly in the LMW forms, whereas the chaperone function predominates in the HMW complexes. The multimeric structures of AtTrx-h3 are regulated not only by heat-shock but also by redox status. Two active Cys residues in AtTrx-h3 are required for disulfide reductase activity, but not for chaperone function. AtTrx-h3 confers enhanced heat-shock tolerance in Arabidopsis, primarily through its chaperone function.






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