Molecular evolution of the domain structures of protein disulfide isomerases

被引:37
作者
Kanai, S
Toh, H
Hayano, T
Kikuchi, M
机构
[1] Biomol Engn Res Inst, Dept Bioinformat, Suita, Osaka 565, Japan
[2] Tonen Corp, Corp Res & Dev Lab, Fundamental Res Labs, Environm Res Grp, Ohi, Saitama 365, Japan
[3] Ristumeikan Univ, Fac Sci & Engn, Dept Biosci & Technol, Kusatsu, Shiga 52577, Japan
关键词
evolution; protein; protein disulfide isomerase; thioredoxin;
D O I
10.1007/PL00006377
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein disulfide isomerase (PDI) is an enzyme that promotes protein folding by catalyzing disulfide bridge isomerization. PDI and its relatives form a diverse protein family whose members are characterized by thioredoxin-like (TX) domains in the primary structures. The family was classified into four classes by the number and the relative positions of the TX domains. To investigate the evolution of the domain structures, we aligned the amino acid sequences of the TX domains, and the molecular phylogeny was examined by the NJ and ML methods. We found that all of the current members of the PDI family have evolved from an ancestral enzyme, which has two TX domains in the primary structure. The diverse domain structures of the members have been generated through domain duplications and deletions.
引用
收藏
页码:200 / 210
页数:11
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