AIM10/YER087W Summary 
AIM10 BASIC INFORMATION
| Standard Name | AIM10 1 |
|---|---|
| Systematic Name | YER087W |
| Feature Type | ORF, Verified |
| Description | Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss (1, 2, 3, 4 and see Summary Paragraph) 
|
| Name Description | Altered Inheritance rate of Mitochondria 1 |
| GO Annotations | All AIM10 GO evidence and references |
|---|---|
| View Computational GO annotations for AIM10 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated |
|
| Cellular Component | |
| High-throughput |
| Interactions | AIM10 All interactions details and references |
|---|---|
| 25 total interaction(s) for 25 unique genes/features. | |
| Genetic Interactions |
|
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000000889 |
|---|
AIM10 RESOURCES
| SGD ORF map | GBrowse |
|---|---|
|
Click on histogram for expression summary
Expression Summary
ADDITIONAL INFORMATION for AIM10
SUMMARY PARAGRAPH for AIM10
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 AIM10]
| 1) | Hess DC, et al. (2009) Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis. PLoS Genet 5(3):e1000407 |
| 2) | Sentandreu M, et al. (1997) Isolation of a putative prolyl-tRNA synthetase (CaPRS) gene from Candida albicans. Yeast 13(14):1375-81 |
| 3) | Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 |
| 4) | Reinders J, et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54 |
| 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 |
