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Gene Review

TYS1  -  tyrosine--tRNA ligase TYS1

Saccharomyces cerevisiae S288c

Synonyms: G7522, MGM104, TyrRS, Tyrosine--tRNA ligase, cytoplasmic, Tyrosyl-tRNA synthetase, ...
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Disease relevance of TYS1


High impact information on TYS1

  • Biochemical experiments and genetic complementation in yeast show partial loss of aminoacylation activity of the mutant proteins, and mutations in YARS, or in its yeast ortholog TYS1, reduce yeast growth [4].
  • Here we show that in vitro transcription of the yeast SUP4 tRNATyr gene in crude yeast extracts is strongly stimulated by tyrosyl-tRNA synthetase (TyrRS) but not by two other non-cognate synthetases [5].
  • However, plasmids carrying the yeast TyrRS gene could not be stably maintained in E. coli [1].
  • Expression of this protein in E. coli demonstrated that tyrosine was incorporated during suppression and that yeast cytoplasmic TyrRS activity was produced [6].
  • Noticeable, yeast TyrRS efficiently charges a variant of E. coli tRNA(Tyr) with a large extra-region provided its G1-C72 base pair is changed to a C1-G72 base pair [7].

Biological context of TYS1

  • TYS1 was reported previously to lie on chromosome XV based on sequence overlap with the adjacent UBR1 gene [8].
  • A search of the nucleotide sequence databases revealed that SSU71 is immediately adjacent to the TYS1 gene, which encodes tRNA(Tyr) synthetase [8].
  • In addition, it is shown that the efficiency of spores formation was drastically reduced in diploid cells homozygous for the disruption of KNR4 or for a temperature-sensitive mutation of TYS1, although this effect could be independent of their protein interaction [9].
  • Using in vitro tRNA transcripts and minihelices it was shown that the tyrosine identity for tRNA charging by tyrosyl-tRNA synthetase (TyrRS) from the archaeon Methanococcus jannaschii is determined by six nucleotides: the discriminator base A73 and the first base-pair C1-G72 in the acceptor stem together with the anticodon triplet [10].
  • One third of genes (13 from 42) in TyrRS gene cluster are responsible for the functions directly related to cell wall assembly and maintenance during sporulation [11].

Anatomical context of TYS1


Associations of TYS1 with chemical compounds


Analytical, diagnostic and therapeutic context of TYS1

  • By using error-prone PCR, we have isolated and characterized three mutants of yeast TyrRS, which can be stably expressed in E. coli [1].
  • By sequence alignments we predicted a Tys1p nuclear localization sequence and showed it to be sufficient for nuclear location of a passenger protein [13].


  1. Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria. Kowal, A.K., Kohrer, C., RajBhandary, U.L. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  2. Changing the amino acid specificity of yeast tyrosyl-tRNA synthetase by genetic engineering. Ohno, S., Yokogawa, T., Nishikawa, K. J. Biochem. (2001) [Pubmed]
  3. Specific tyrosylation of the bulky tRNA-like structure of brome mosaic virus RNA relies solely on identity nucleotides present in its amino acid-accepting domain. Fechter, P., Giegé, R., Rudinger-Thirion, J. J. Mol. Biol. (2001) [Pubmed]
  4. Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy. Jordanova, A., Irobi, J., Thomas, F.P., Van Dijck, P., Meerschaert, K., Dewil, M., Dierick, I., Jacobs, A., De Vriendt, E., Guergueltcheva, V., Rao, C.V., Tournev, I., Gondim, F.A., D'Hooghe, M., Van Gerwen, V., Callaerts, P., Van Den Bosch, L., Timmermans, J.P., Robberecht, W., Gettemans, J., Thevelein, J.M., De Jonghe, P., Kremensky, I., Timmerman, V. Nat. Genet. (2006) [Pubmed]
  5. Stimulation of transcription of the yeast tRNATyr gene in cell-free extracts by tyrosyl-tRNA synthetase. Smagowicz, W., Ruet, A., Camier, S., Sentenac, A., Fromageot, P., Sternbach, H. Nature (1983) [Pubmed]
  6. Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene. Isolation by complementation of a mutant Escherichia coli suppressor tRNA defective in aminoacylation and sequence analysis. Chow, C.M., RajBhandary, U.L. J. Biol. Chem. (1993) [Pubmed]
  7. Identity of tRNA for yeast tyrosyl-tRNA synthetase: tyrosylation is more sensitive to identity nucleotides than to structural features. Fechter, P., Rudinger-Thirion, J., Théobald-Dietrich, A., Giegé, R. Biochemistry (2000) [Pubmed]
  8. SSU71, encoding the largest subunit of TFIIF, is located on the right arm of chromosome VII in Saccharomyces cerevisiae. Sun, Z.W., Hampsey, M. Yeast (1995) [Pubmed]
  9. Interaction of Knr4 protein, a protein involved in cell wall synthesis, with tyrosine tRNA synthetase encoded by TYS1 in Saccharomyces cerevisiae. Dagkessamanskaia, A., Martin-Yken, H., Basmaji, F., Briza, P., Francois, J. FEMS Microbiol. Lett. (2001) [Pubmed]
  10. Major tyrosine identity determinants in Methanococcus jannaschii and Saccharomyces cerevisiae tRNA(Tyr) are conserved but expressed differently. Fechter, P., Rudinger-Thirion, J., Tukalo, M., Giegé, R. Eur. J. Biochem. (2001) [Pubmed]
  11. Bioinformatic analysis of changes in expression level of tyrosyl-tRNA synthetase during sporulation process in Saccharomyces cerevisiae. Ivakhno, S.S., Kornelyuk, A.I. Mikrobiol. Z. (2005) [Pubmed]
  12. Structural analyses on yeast tRNA(Tyr) and its complex with tyrosyl-tRNA synthetase by the use of hydroxyl radical 'footprinting'. Motoki, I., Yosinari, S., Watanabe, K., Nishikawa, K. Nucleic Acids Symp. Ser. (1991) [Pubmed]
  13. Role of nuclear pools of aminoacyl-tRNA synthetases in tRNA nuclear export. Azad, A.K., Stanford, D.R., Sarkar, S., Hopper, A.K. Mol. Biol. Cell (2001) [Pubmed]
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