Amino acid sequence diversities in TBP, TATA binding protein, of extremely halophilic archaeon Haloarcula japonica strain TR-1
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The TATA-box binding protein (TBP) is a basal transcription factor involved in transcription initiation in Eukarya and Archaea. Through exhaustive analyses of the whole geneme of extremely halophilic archaeon, Haloarcula japonica strain TR-1, six TBP genes were found and structurally analyzed. These TBPs were designated as TBP1, TBP2, TBP3, TBP4, TBP5 and TBP6, respectively and these TBPs were diverged from other archaeal TBPs that have been known. TBP1 gene was found to encode a polypeptide consisting of 182 amino acid residues, showing 35.0％ identity to that of H. marismortui. TBP2 gene was found to encode a polypeptide consisting of 182 amino acid residues, showing 36.5％ identity to that of H. marismortui. TBP3 gene was found to encode a polypeptide consisting of 186 amino acid residues, showing 100％ identity to that of H. marismortui. TBP4 gene was found to encode a polypeptide consisting of 185 amino acid residues, showing 42.9％ identity to that of H. marismortui. TBP5 gene was found to encode a polypeptide consisting of 182 amino acid residues, showing 35.4％ identity to that of H. marismortui. TBP6 gene was found to encode a polypeptide consisting of 182 amino acid residues, showing 46.1％ identity to that of H. marismortui. By phylogenetic analyses of these six proteins, TBP3 is conserved in amino acid sequence with other archaeal strains including methanogens and thermophiles, It may suggest that the TBP3 is core TBP function in transcriptional initiation such as housekeeping genes. Six histidine-tagged version of the H. japonica TBPs were produced in Escherichia coli in a denature conditions after construction of overexpression plasmids and purified by means of Ni-chelating chromatography.
- 近畿大学工学部の論文
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