GLN4/YOR168W Summary 
GLN4 BASIC INFORMATION
| Standard Name | GLN4 |
|---|---|
| Systematic Name | YOR168W |
| Feature Type | ORF, Verified |
| Description | Glutamine tRNA synthetase, monomeric class I tRNA synthetase that catalyzes the specific glutaminylation of tRNA(Glu); N-terminal domain proposed to be involved in enzyme-tRNA interactions (1, 2, 3 and see Summary Paragraph) 
|
| Name Description | GLutamiNe metabolism |
| Gene Product Alias | glutamyl-tRNA synthetase 1 |
| GO Annotations | All GLN4 GO evidence and references |
|---|---|
| View Computational GO annotations for GLN4 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Mutant Phenotype | All GLN4 Phenotype details and references |
|---|---|
| Large-scale survey | |
| null | |
| overexpression | |
| repressible |
| Interactions | GLN4 All interactions details and references |
|---|---|
| 10 total interaction(s) for 10 unique genes/features. | |
| Physical Interactions |
|
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000005694 |
|---|
GLN4 RESOURCES
| SGD ORF map | GBrowse |
|---|---|
|
Click on histogram for expression summary
Expression Summary
ADDITIONAL INFORMATION for GLN4
SUMMARY PARAGRAPH for GLN4
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 (4, 5 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 (4, 5, 6 and references therein).
Last updated: 2008-07-14
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for GLN4]
| 1) | Ludmerer SW and Schimmel P (1985) Cloning of GLN4: an essential gene that encodes glutaminyl-tRNA synthetase in Saccharomyces cerevisiae. J Bacteriol 163(2):763-8 |
| 2) | Ludmerer SW, et al. (1993) Purification of glutamine tRNA synthetase from Saccharomyces cerevisiae. A monomeric aminoacyl-tRNA synthetase with a large and dispensable NH2-terminal domain. J Biol Chem 268(8):5519-23 |
| 3) | Whelihan EF and Schimmel P (1997) Rescuing an essential enzyme-RNA complex with a non-essential appended domain. EMBO J 16(10):2968-74 |
| 4) | Delarue M (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55 |
| 5) | Arnez JG and Moras D (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6 |
| 6) | 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 |
