[Comparative analysis of primary structures of yeast dolicholphosphomannosyl- and dolichophosphoglucosyl synthetases and other dolichol-conjugated enzymes].

Primary structure of yeast dolicholphosphomannosyl- (DPMS) and dolicholphosphoglucosylsynthetases (DPGS) have been compared both between themselves and DPMS and DPGS with yeast beta- and alpha-1, 3-mannosyltransferases, glucosyltransferases and rat mannosyl-binding proteins. The long homological segments were revealed. The homological segments of beta- and alpha-1, 3-mannosyltransferases were located in regions having potency to form coiled-coil structures. These structures are known to be included in carbohydrate-binding protein domains. The previous data and the results presented now have made it possible to conclude that the dolichol-coupled enzymes have evolutionary relationship between themselves and common evolutionary roots with carbohydrate-binding proteins (lectins).