Abstract
The core structure of membrane lipids of archaea have some unique properties that permit archaea to be distinguished from the others, i.e. bacteria and eukaryotes. (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase, which catalyzes the transfer of a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate, is involved in the biosynthesis of archaeal membrane lipids. Enzymes of the UbiA prenyltransferase family are known to catalyze the transfer of a prenyl group to various acceptors with hydrophobic ring structures in the biosynthesis of respiratory quinones, hemes, chlorophylls, vitamin E, and shikonin. The thermoacidophilic archaeon Sulfolobus solfataricus was found to encode three homologues of UbiA prenyltransferase in its genome. One of the homologues encoded by SSO0583 was expressed in Escherichia coli, purified, and characterized. Radio-assay and mass spectrometry analysis data indicated that the enzyme specifically catalyzes the biosynthesis of (S)-2,3-di-O-geranylgeranylglyceryl phosphate. The fact that the orthologues of the enzyme are encoded in almost all archaeal genomes clearly indicates the importance of their functions. A phylogenetic tree constructed using the amino acid sequences of some typical members of the UbiA prenyltransferase family and their homologues from S. solfataricus suggests that the two other S. solfataricus homologues, excluding the (S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase, are involved in the production of respiratory quinone and heme, respectively. We propose here that archaeal prenyltransferases involved in membrane lipid biosynthesis might be prototypes of the protein family and that archaea might have played an important role in the molecular evolution of prenyltransferases.
Highlights
The core structure of membrane lipids of archaea have some unique properties that permit archaea to be distinguished from the others, i.e. bacteria and eukaryotes. (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase, which catalyzes the transfer of a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate, is involved in the biosynthesis of archaeal membrane lipids
Digeranylgeranylglyceryl Phosphate Synthase thase (DGGGPS), further information concerning this prenyltransferase has not been obtained at this time
Based on a sequence alignment and phylogenetic analysis, DGGGPS appeared to be a member of a large family of proteins, i.e. the UbiA prenyltransferase family, which consists of prenyltransferases that are involved in the biosyntheses of respiratory quinones, hemes, chlorophylls, vitamin E, and shikonin
Summary
Thase (DGGGPS), further information concerning this prenyltransferase has not been obtained at this time. DGGGP, which has been shown to be the intermediate of archaeal membrane lipids, as evidenced by an incorporation experiment by Eguchi et al [15], would be expected to subsequently undergo saturation of the alkyl group, modification of the polar head group, and the formation of the cyclic tetraether structure [16]. Comprehensive information concerning these biosynthetic reactions is not available: the genes and proteins involved and even the order of the reactions are unknown at this time, expect for some enzymes that catalyze the modification of polar head groups [17, 18]. The gene was cloned and expressed in Escherichia coli, and the recombinantly expressed enzyme was shown to catalyze the formation of DGGGP from GGGP and GGPP. Based on a sequence alignment and phylogenetic analysis, DGGGPS appeared to be a member of a large family of proteins, i.e. the UbiA prenyltransferase family, which consists of prenyltransferases that are involved in the biosyntheses of respiratory quinones, hemes, chlorophylls, vitamin E, and shikonin
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