Disease relevance of TYS1

• This lack of stability is most likely due to the fact that the wild-type yeast TyrRS misaminoacylates the E. coli proline tRNA [1].
• In an attempt to generate mutant aminoacyl-tRNA synthetases capable of charging non-canonical amino acids, a series of yeast tyrosyl-tRNA synthetase (TyrRS) mutants was constructed by site-specific mutagenesis of putative active site residues, which were deduced by analogy with those of Bacillus stearothermophilus TyrRS [2].
• Residues specifying aminoacylation by yeast tyrosyl-tRNA synthetase (TyrRS) of the tRNA-like structure present at the 3'-end of brome mosaic virus (BMV) RNA were determined by the in vitro approach using phage T7 transcripts [3].

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

• Interaction of Knr4 protein, a protein involved in cell wall synthesis, with tyrosine tRNA synthetase encoded by TYS1 in Saccharomyces cerevisiae [9].

Associations of TYS1 with chemical compounds

• On the other hand, the ability to utilize 3-iodo-L-tyrosine was newly generated in this mutant TyrRS, since the wild-type TyrRS could not accept 3-iodo-L-tyrosine at all under physiological conditions [2].
• Furthermore, the cell wall biogenesis protein KNR4 which physically interacts with TyrRS and cooperates in beta-1,3 glucan biosynthesis falls into a single gene cluster with TyrRS [11].
• Hydroxyl radical, generated by reduction of hydrogen peroxide by Fe(II)-EDTA, was used to investigate the contact sites of yeast tRNA(Tyr) with its cognate tyrosyl-tRNA synthetase (TyrRS) [12].

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].

References