ILS1/YBL076C Summary 
ILS1 BASIC INFORMATION
| Standard Name | ILS1 1 |
|---|---|
| Systematic Name | YBL076C |
| Feature Type | ORF, Verified |
| Description | Cytoplasmic isoleucine-tRNA synthetase, target of the G1-specific inhibitor reveromycin A (2, 3 and see Summary Paragraph) 
|
| Name Description | IsoLeucine-tRNA Synthetase |
| Gene Product Alias | isoleucyl-tRNA synthetase 4 |
| GO Annotations | All ILS1 GO evidence and references |
|---|---|
| View Computational GO annotations for ILS1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Mutant Phenotype | All ILS1 Phenotype details and references |
|---|---|
| Large-scale survey | |
| null |
| Interactions | ILS1 All interactions details and references |
|---|---|
| 25 total interaction(s) for 23 unique genes/features. | |
| Physical Interactions |
|
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000000172 |
|---|
ILS1 RESOURCES
| SGD ORF map | GBrowse |
|---|---|
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Click on histogram for expression summary
Expression Summary
ADDITIONAL INFORMATION for ILS1
SUMMARY PARAGRAPH for ILS1
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 (5, 6 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 (5, 6, 7 and references therein).
Last updated: 2008-07-14
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for ILS1]
| 1) | Nelbock, P., et al. (1989) ; Personal Communication, Mortimer Map Edition 10 |
| 2) | Englisch U, et al. (1987) Structure of the yeast isoleucyl-tRNA synthetase gene (ILS1). DNA-sequence, amino-acid sequence of proteolytic peptides of the enzyme and comparison of the structure to those of other known aminoacyl-tRNA synthetases. Biol Chem Hoppe Seyler 368(8):971-9 |
| 3) | Miyamoto Y, et al. (2002) Identification of Saccharomyces cerevisiae isoleucyl-tRNA synthetase as a target of the G1-specific inhibitor Reveromycin A. J Biol Chem 277(32):28810-4 |
| 4) | Meussdoerffer F and Fink GR (1983) Structure and expression of two aminoacyl-tRNA synthetase genes from Saccharomyces cerevisiae. J Biol Chem 258(10):6293-9 |
| 5) | Delarue M (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55 |
| 6) | Arnez JG and Moras D (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6 |
| 7) | 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 |
