A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis

被引:143
作者
Chu, CC
Lee, WC
Guo, WY
Pan, SM
Chen, LJ
Li, HM
Jinn, TL [1 ]
机构
[1] Natl Taiwan Univ, Dept Life Sci, Taipei 10617, Taiwan
[2] Natl Taiwan Univ, Inst Plant Biol, Taipei 10617, Taiwan
[3] Acad Sinica, Inst Mol Biol, Taipei 11529, Taiwan
关键词
D O I
10.1104/pp.105.065284
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The copper chaperone for superoxide dismutase (CCS) has been identified as a key factor integrating copper into copper/zinc superoxide dismutase (CuZnSOD) in yeast ( Saccharomyces cerevisiae) and mammals. In Arabidopsis ( Arabidopsis thaliana), only one putative CCS gene (AtCCS, At1g12520) has been identified. The predicted AtCCS polypeptide contains three distinct domains: a central domain, flanked by an ATX1-like domain, and a C-terminal domain. The ATX1-like and C-terminal domains contain putative copper-binding motifs. We have investigated the function of this putative AtCCS gene and shown that a cDNA encoding the open reading frame predicted by The Arabidopsis Information Resource complemented only the cytosolic and peroxisomal CuZnSOD activities in the Atccs knockout mutant, which has lost all CuZnSOD activities. However, a longer AtCCS cDNA, as predicted by the Munich Information Centre for Protein Sequences and encoding an extra 66 amino acids at the N terminus, could restore all three, including the chloroplastic CuZnSOD activities in the Atccs mutant. The extra 66 amino acids were shown to direct the import of AtCCS into chloroplasts. Our results indicated that one AtCCS gene was responsible for the activation of all three types of CuZnSOD activity. In addition, a truncated AtCCS, containing only the central and C-terminal domains without the ATX1-like domain failed to restore any CuZnSOD activity in the Atccs mutant. This result indicates that the ATX1-like domain is essential for the copper chaperone function of AtCCS in planta.
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收藏
页码:425 / 436
页数:12
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