GRS1 BASIC INFORMATION
| Standard Name | GRS1 |
|---|---|
| Systematic Name | YBR121C |
| Feature Type | ORF, Verified |
| Description | Cytoplasmic and mitochondrial glycyl-tRNA synthase that ligates glycine to the cognate anticodon bearing tRNA; transcription termination factor that may interact with the 3'-end of pre-mRNA to promote 3'-end formation (1, 2 and see Summary Paragraph)
|
| Name Description | Glycyl-tRNA Synthase 2 |
| Gene Product Alias | glycyl-tRNA synthetase 2 |
| GO Annotations | All GRS1 GO evidence and references |
|---|---|
| View Computational GO annotations for GRS1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
|
| High-throughput |
| Mutant Phenotype | All GRS1 Phenotype details and references |
|---|---|
| Classical genetics | |
| reduction of function | |
| Large-scale survey | |
| conditional | |
| null | |
| overexpression |
| Interactions | GRS1 All interactions details and references |
|---|---|
| 25 total interaction(s) for 22 unique genes/features. | |
| Physical Interactions |
|
| Genetic Interactions |
|
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000000325 |
|---|
ADDITIONAL INFORMATION for GRS1
SUMMARY PARAGRAPH for GRS1
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 (3, 4 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 (3, 4, 5 and references therein).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for GRS1]
| 1) | Turner RJ, et al. (2000) One of two genes encoding glycyl-tRNA synthetase in Saccharomyces cerevisiae provides mitochondrial and cytoplasmic functions. J Biol Chem 275(36):27681-8 |
| 2) | Magrath C and Hyman LE (1999) A mutation in GRS1, a glycyl-tRNA synthetase, affects 3'-end formation in Saccharomyces cerevisiae. Genetics 152(1):129-41 |
| 3) | Delarue M (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55 |
| 4) | Arnez JG and Moras D (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6 |
| 5) | 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 |




