Multiple isoforms of Arabidopsis thaliana h-type thioredoxins (AtTrx-hs) have distinct structural and functional specificities. AtTrx-h3 acts as both a disulfide reductase and as a molecular chaperone. We prepared five representative AtTrx-hs and compared their protein structures and disulfide reductase and molecular chaperone activities. AtTrx-h2 with an N-terminal extension exhibited distinct functional properties with respect to other AtTrx-hs. AtTrx-h2 formed low-molecular-mass structures and exhibited only disulfide reductase activity, whereas the other AtTrx-h isoforms formed high-molecular-mass complexes and displayed both disulfide reductase and molecular chaperone activities. The domains that determine the unique structural and functional properties of each AtTrx-hs protein were determined by constructing a domain-swap between the N- and C-terminal regions of AtTrx-h2 and AtTrx-h3 (designated AtTrx-h-2N3C and AtTrx-h-3N2C respectively), an N-terminal deletion mutant of AtTrx-h2 [AtTrx-h2-N(∆19)] and site-directed mutagenesis of AtTrx-h3. AtTrx-h2-N(∆19) and AtTrx-h-3N2C exhibited similar properties to those of AtTrx-h2, but AtTrx-h-2N3C behaved more like AtTrx-h3, suggesting that the structural and functional specificities of AtTrx-hs are determined by their C-terminal regions. Hydrophobicity profiling and molecular modelling revealed that Ala100 and Ala106 in AtTrx-h3 play critical roles in its structural and functional regulation. When these two residues in AtTrx-h3 were replaced with lysine, AtTrx-h3 functioned like AtTrx-h2. The chaperone function of AtTrx-hs conferred enhanced heat-shock-resistance on a thermosensitive trx1/2-null yeast mutant.
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Research Article|
October 24 2013
Analysis of Arabidopsis thioredoxin-h isotypes identifies discrete domains that confer specific structural and functional properties
Young Jun Jung;
Young Jun Jung
1
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Yong Hun Chi;
Yong Hun Chi
1
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Ho Byoung Chae;
Ho Byoung Chae
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Mi Rim Shin;
Mi Rim Shin
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Eun Seon Lee;
Eun Seon Lee
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Joon-Yung Cha;
Joon-Yung Cha
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Seol Ki Paeng;
Seol Ki Paeng
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Yuno Lee;
Yuno Lee
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Jin Ho Park;
Jin Ho Park
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Woe Yeon Kim;
Woe Yeon Kim
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Chang Ho Kang;
Chang Ho Kang
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Kyun Oh Lee;
Kyun Oh Lee
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Keun Woo Lee;
Keun Woo Lee
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Dae-Jin Yun;
Dae-Jin Yun
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
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Sang Yeol Lee
Sang Yeol Lee
2
*Division of Applied Life Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea
2To whom correspondence should be addressed (email sylee@gnu.ac.kr).
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Publisher: Portland Press Ltd
Received:
May 02 2013
Revision Received:
September 03 2013
Accepted:
September 05 2013
Accepted Manuscript online:
September 05 2013
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem J (2013) 456 (1): 13–24.
Article history
Received:
May 02 2013
Revision Received:
September 03 2013
Accepted:
September 05 2013
Accepted Manuscript online:
September 05 2013
Citation
Young Jun Jung, Yong Hun Chi, Ho Byoung Chae, Mi Rim Shin, Eun Seon Lee, Joon-Yung Cha, Seol Ki Paeng, Yuno Lee, Jin Ho Park, Woe Yeon Kim, Chang Ho Kang, Kyun Oh Lee, Keun Woo Lee, Dae-Jin Yun, Sang Yeol Lee; Analysis of Arabidopsis thioredoxin-h isotypes identifies discrete domains that confer specific structural and functional properties. Biochem J 15 November 2013; 456 (1): 13–24. doi: https://doi.org/10.1042/BJ20130618
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