Molecular evolution of the domain structures of protein disulfide isomerases.
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.
Department of Bioinfomatics, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka, 565 Japan. skanai@beri.co.jp
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Kanai
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Toh
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Hayano
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Kikuchi
D019143:Evolution, Molecular; D008957:Models, Genetic; D010802:Phylogeny; D011336:Probability; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases / Q000145:classification / Q000235:genetics*; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D013879:Thioredoxins / Q000235:genetics
D013879:Thioredoxins; D019704:Protein Disulfide-Isomerases