Premium
Arabidopsis mitochondrial voltage‐dependent anion channel 3 (AtVDAC3) protein interacts with thioredoxin m2
Author(s) -
Zhang Min,
Takano Tetsuo,
Liu Shenkui,
Zhang Xinxin
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.03.034
Subject(s) - voltage dependent anion channel , thioredoxin , arabidopsis , chemistry , microbiology and biotechnology , biochemistry , biophysics , biology , gene , escherichia coli , bacterial outer membrane , mutant
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 H 2 O 2 accumulation, while AtTrx m2 overexpression conferred resistance to NaCl and reduced H 2 O 2 . Results indicate that both AtVDAC3 and AtTrx m2 are involved in ROS signaling and play opposite roles in NaCl stress response.