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FEBS Lett. 2015 May 8;589(11):1207-13. doi: 10.1016/j.febslet.2015.03.034. Epub 2015 Apr 8.

Arabidopsis mitochondrial voltage-dependent anion channel 3 (AtVDAC3) protein interacts with thioredoxin m2.

Author information

1
Key Laboratory of Saline-alkali Vegetation Ecology Restoration in Oil Field (SAVER), Ministry of Education, Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University, Harbin 150040, China.
2
Asian Natural Environment Science Center (ANESC), The University of Tokyo, 1-1-1 Midori Cho, Nishitokyo-shi, Tokyo 188-0002, Japan.
3
Key Laboratory of Saline-alkali Vegetation Ecology Restoration in Oil Field (SAVER), Ministry of Education, Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University, Harbin 150040, China. Electronic address: xxzhang@nefu.edu.cn.

Abstract

Voltage-dependent anion channels (VDACs) are conserved mitochondrial outer membrane proteins. A yeast two-hybrid screen identified interaction between Arabidopsis VDAC3 and the chloroplast protein thioredoxin m2 (AtTrx m2). This was confirmed via pull-down assay. A bimolecular fluorescence complementation assay located the interaction in mitochondria. AtVDAC3 and AtTrx m2 transcripts were expressed in multiple tissues and up-regulated by abiotic stress. Under NaCl stress, AtVDAC3 overexpression inhibited growth and increased H2O2 accumulation, while AtTrx m2 overexpression conferred resistance to NaCl and reduced H2O2. Results indicate that both AtVDAC3 and AtTrx m2 are involved in ROS signaling and play opposite roles in NaCl stress response.

KEYWORDS:

Chloroplast thioredoxin; Mitochondrial voltage-dependent anion channel; NaCl stress; Protein interaction

PMID:
25862497
DOI:
10.1016/j.febslet.2015.03.034
[Indexed for MEDLINE]
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