Biopolym. Cell. 2004; 20(1-2):144-149.
Molecular cloning, sequencing and sequence analysis of Thermus thermophilus tyrosyl-tRNA synthetase
1, 2Yaremchuk A. D., 1Kovalenko O. P., 1Gudzera O. I., 1, 2Tukalo M. A.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. EMBL
    6, rue Jules Horowitz, 38042 Grenoble Cedex 9, France


The gene encoding tyrosyl-tRNA synthetase (TyrRS) from the extreme thermophilic eubacterium T. thermophilus HB27 has been cloned and sequenced. The open reading frame encodes a polypeptide chain of 432 amino acid residues in length (molecular mass 48717 Da). Comparison of the amino acid sequence of the T. thermophilus TyrRS (TyrRSTT) with those of TyrRS from various organisms shows that T. thermophilus enzyme shares a branch in the philogenetic tree of eubacterial TyrRSs with the enzymes from Aquifex aeolicus, Deinococcus radiodurans, Haemophilus influenzae and Helicobacter pyroly (40-57 % amino acid identity), distinct from the branch containing Esherichia coli, Chlamydia trachomatis and Bacillus stearothermophilus, for example (24–28 % amino acid identity). The TyrRS active site domain is highly conserved, whereas a C-terminal tRNA binding domain contains only few conserved residues. But even in the active site exists one very important difference between the two groups of bacterial TyrRSs: Lys-41 in TyrRSTT (and in TyrRS from many human pathogenic bacteria) is conserved as a tyrosine in another group of bacterial TyrRSs and eukaryotic sequences including human. This knowledge could be exploited in the design of new antibiotics.


[1] Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 1990;347(6289):203-6.
[2] Cusack S, Berthet-Colominas C, Hartlein M, Nassar N, Leberman R. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A. Nature. 1990;347(6290):249-55.
[3] Steinberg S, Misch A, Sprinzl M. Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res. 1993;21(13):3011-5.
[4] Quinn CL, Tao N, Schimmel P. Species-specific microhelix aminoacylation by a eukaryotic pathogen tRNA synthetase dependent on a single base pair. Biochemistry. 1995;34(39):12489-95.
[5] Iaremchuk AD, Tukalo MA, Egorova SP, Konovalenko AV, Matsuka GKh. Isolation of tyrosyl-tRNA-synthetase from Thermus thermophilus HB-27. Ukr Biokhim Zh. 1990;62(2):97-9.
[6] Marmur J. A procedure for the isolation of deoxyribonucleic acid from micro-organisms J. Mol. Biol. 1961; 3(2)208-218.
[7] Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977;74(12):5463-7.
[8] Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S. Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J. 2002;21(14):3829-40.
[9] Qiu X, Janson CA, Smith WW, Green SM, McDevitt P, Johanson K, Carter P, Hibbs M, Lewis C, Chalker A, Fosberry A, Lalonde J, Berge J, Brown P, Houge-Frydrych CS, Jarvest RL. Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors. Protein Sci. 2001;10(10):2008-16.
[10] Kim S, Lee SW, Choi EC, Choi SY. Aminoacyl-tRNA synthetases and their inhibitors as a novel family of antibiotics. Appl Microbiol Biotechnol. 2003;61(4):278-88.