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Structure of the phenylalanyl-tRNA synthetase genes from Thermus thermophilus HB8 and their expression in Escherichia coli

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Item Type:Article
Title:Structure of the phenylalanyl-tRNA synthetase genes from Thermus thermophilus HB8 and their expression in Escherichia coli
Creators Name:Kreutzer, R., Kruft, V., Bobkova, E.V., Lavrik, O.I. and Sprinzl, M.
Abstract:A 4459 bp long BamHI restriction fragment containing the two genes for the Thermus thermophilus HB8 phenylalanyl-tRNA synthetase was cloned in Escherichia coli and its nucleotide sequence was determined. The genes pheS and pheT encode the alpha- and beta-subunits with a molecular weight of 39 and 87 kD, respectively. Three conserved sequence motifs typical for class II tRNA synthetases occur in the alpha-subunit. Secondary structure predictions indicate that an arm composed of two anti-parallel alpha-helices similar to that reported for the E.coli seryl-tRNA synthetase may be present in its N-terminal portion. In the beta-subunit clusters of hydrophilic amino acids and a leucine zipper motif were identified, and several pronounced alpha-helical regions were predicted. The particular arginine and lysine residues in the N-terminal portion of the beta-subunit, which were found to participate in tRNA binding in the yeast and E.coli PheRSs, have their counterparts in the T.thermophilus protein. The 5'-portion of an open reading frame downstream of pheT was found and codes for a yet unidentified, extremely hydrophobic peptide. The pheST genes are presumably cotranscribed and translationally coupled. A novel type of a putative transcriptional terminator in Thermus species was identified immediately downstream of pheT and other Thermus genes. The genes pheS and pheST were expressed in E.coli.
Keywords:Amino Acid Sequence, Base Sequence, Molecular Cloning, Escherichia coli, Bacterial Gene Expression Regulation, Molecular Sequence Data, Phenylalanine-tRNA Ligase, Plasmids, Restriction Mapping, Thermus thermophilus
Source:Nucleic Acids Research
Publisher:Oxford University Press
Page Range:4173-4178
Date:25 August 1992
Official Publication:https://doi.org/10.1093/nar/20.16.4173
PubMed:View item in PubMed

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