Nucleic Acids Research, 1992, Vol. 20, No. 16 4173-4178
© 1992
MOLECULAR BIOLOGY |
Structure of the phenylalnyl-tRNA synthetase genes from Thermus thermophilus HB8 and their expression in Escherichia coli
Laboratorium für Biochemie, Universität Bayreuth, Universitätstraße 30 8580 Bayreuth 1Max-Planck-Institute für Molekulare Genetik Abteilung Wittmann, Ihnestraße 73, 1000 Berlin 33, Germany 2Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences Lavrentiev Prospect 8, 630090 Novosibirsk, Russia
*To whom correspondence should be addressed
Received June 5, 1992. Revised July 24, 1992. Accepted July 24, 1992.
A 4459 bp long BamHI restriction fragment containing the two genes for the Thermus thermophilus HB8 phenylalanyt-tRNA synthetase was cloned in Escherichia coll and its nucleotlde sequence was determined. The genes pheS and pheT encode the 
- and ß-subunlts with a molecular weight of 39 and 87 kD, respectively. Three conserved sequence motifs typical for class II tRNA synthetases occur in the -subunit. Secondary structurepredictions indicate that an arm composed of two antiparallel -helices similar to that reported for the E.coll seryl-tRNA synthetase may be present in its N-terminal portion. In the ß-subunlt clusters of hydrophillc amino acids and a leucine zipper motif were identified, and several pronounced -hellcal regions were predicted. The particular arginine and lyslne residues in the N-terminal portion of the ß-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 peptkte. The pheST genes are presumably cotranscribed and translatlonally 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.
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