TYS1/YGR185C Summary Help

Standard Name TYS1 1
Systematic Name YGR185C
Alias TTS1 2
Feature Type ORF, Verified
Description Cytoplasmic tyrosyl-tRNA synthetase; required for cytoplasmic protein synthesis; interacts with positions 34 and 35 of the tRNATyr anticodon; mutations in human ortholog YARS are associated with Charcot-Marie-Tooth (CMT) neuropathies; protein abundance increases in response to DNA replication stress (2, 3, 4, 5, 6, 7 and see Summary Paragraph)
Also known as: TyrRS 8
Name Description TYrosyl-tRNA Synthetase 1
Chromosomal Location
ChrVII:867520 to 866336 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All TYS1 GO evidence and references
  View Computational GO annotations for TYS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 10 genes
Classical genetics
Large-scale survey
reduction of function
118 total interaction(s) for 106 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-RNA: 4
  • Affinity Capture-Western: 2
  • PCA: 1
  • Reconstituted Complex: 3
  • Two-hybrid: 4

Genetic Interactions
  • Negative Genetic: 76
  • Positive Genetic: 5
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2

Expression Summary
Length (a.a.) 394
Molecular Weight (Da) 44,020
Isoelectric Point (pI) 8.75
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:867520 to 866336 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1185 867520..866336 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003417

About aminoacyl-tRNA synthetases...

In a process critical for accurate translation of the genetic code, aminoacyl-tRNA synthetases (aka aminoacyl-tRNA ligases) attach amino acids specifically to cognate tRNAs, thereby "charging" the tRNAs. The catalysis is accomplished via a two-step mechanism. First, the synthetase activates the amino acid in an ATP-dependent reaction, producing aminoacyl-adenylate and releasing inorganic pyrophosphate (PPi). Second, the enzyme binds the correct tRNA and transfers the activated amino acid to either the 2' or 3' terminal hydroxyl group of the tRNA, forming the aminoacyl-tRNA and AMP (9, 10 and references therein).

Aminoacyl-tRNA synthetases possess precise substrate specificity and, despite their similarity in function, vary in size, primary sequence and subunit composition. Individual members of the aminoacyl-tRNA synthetase family can be categorized in one of two classes, depending on amino acid specificity. Class I enzymes (those specific for Glu, Gln, Arg, Cys, Met, Val, Ile, Leu, Tyr and Trp) typically contain two highly conserved sequence motifs, are monomeric or dimeric, and aminoacylate at the 2' terminal hydroxyl of the appropriate tRNA. Class II enzymes (those specific for Gly, Ala, Pro, Ser, Thr, His, Asp, Asn, Lys and Phe) typically contain three highly conserved sequence motifs, are dimeric or tetrameric, and aminoacylate at the 3' terminal hydroxyl of the appropriate tRNA (9, 10, 11 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for TYS1
1) Dagkessamanskaia A, et al.  (2001) Interaction of Knr4 protein, a protein involved in cell wall synthesis, with tyrosine tRNA synthetase encoded by TYS1 in Saccharomyces cerevisiae. FEMS Microbiol Lett 200(1):53-8
2) Guan MX  (1997) Cytoplasmic tyrosyl-tRNA synthetase rescues the defect in mitochondrial genome maintenance caused by the nuclear mutation mgm104-1 in the yeast Saccharomyces cerevisiae. Mol Gen Genet 255(5):525-32
3) Cavarelli J, et al.  (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4
4) Chow CM and RajBhandary UL  (1993) Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene. Isolation by complementation of a mutant Escherichia coli suppressor tRNA defective in aminoacylation and sequence analysis. J Biol Chem 268(17):12855-63
5) Bare LA and Uhlenbeck OC  (1986) Specific substitution into the anticodon loop of yeast tyrosine transfer RNA. Biochemistry 25(19):5825-30
6) Jordanova A, et al.  (2006) Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy. Nat Genet 38(2):197-202
7) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
8) Smagowicz W, et al.  (1983) Stimulation of transcription of the yeast tRNATyr gene in cell-free extracts by tyrosyl-tRNA synthetase. Nature 304(5928):747-9
9) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
10) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
11) Eriani G, et al.  (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347(6289):203-6