| Standard Name | NAM2 1 (see Nomenclature conflict Note) |
|---|---|
| Systematic Name | YLR382C |
| Alias | MSL1 |
| Feature Type | ORF, Verified |
| Description | Mitochondrial leucyl-tRNA synthetase, also has a direct role in splicing of several mitochondrial group I introns; indirectly required for mitochondrial genome maintenance (2, 3, 4, 5 and see Summary Paragraph) |
| Name Description | Nuclear Accommodation of Mitochondria 1 |
| Gene Product Alias | LeuRS 6 , mitochondrial leucyl-tRNA synthetase 6 |
| Chromosomal Location | |
|---|---|
| Note: this feature is encoded on the Crick strand. | |
| Genetic position: 325 cM |
| View Computational GO annotations for NAM2 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| 38 total interaction(s) for 34 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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| Resources |
| Localization | |
|---|---|
| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Genetic position: 325 cM | |||||||||||||
| Last Update | Coordinates: 2004-02-05 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
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| S288C only | |
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| 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 |
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| Primary SGDID | S000004374 |
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NOMENCLATURE CONFLICT NOTE
| Name | Relevance | Description |
|---|---|---|
| MSL1 | Nomenclature conflict | MSL1 has been used in the literature to refer to both NAM2/YLR382C (Tzagoloff, A. et al. (1988) J. Biol. Chem. 263:850; PMID:2826465), which encodes a mitochondrial leucyl tRNA synthetase, and MSL1/YIR009W (Tang, J. et al. (1996) Mol. Cell. Biol. 16:2787; PMID:8649387), which encodes the U2 small nuclear ribonucleoprotein particle B" protein. |
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 (7, 8 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 (7, 8, 9 and references therein).
| 1) | Dujardin G, et al. (1980) Long range control circuits within mitochondria and between nucleus and mitochondria. I. Methodology and phenomenology of suppressors. Mol Gen Genet 179(3):469-82 |
| 2) | Labouesse M (1990) The yeast mitochondrial leucyl-tRNA synthetase is a splicing factor for the excision of several group I introns. Mol Gen Genet 224(2):209-21 |
| 3) | Zagorski W, et al. (1991) Purification and characterization of the Saccharomyces cerevisiae mitochondrial leucyl-tRNA synthetase. J Biol Chem 266(4):2537-41 |
| 4) | Labouesse M, et al. (1985) The yeast nuclear gene NAM2 is essential for mitochondrial DNA integrity and can cure a mitochondrial RNA-maturase deficiency. Cell 41(1):133-43 |
| 5) | Rho SB and Martinis SA (2000) The bI4 group I intron binds directly to both its protein splicing partners, a tRNA synthetase and maturase, to facilitate RNA splicing activity. RNA 6(12):1882-94 |
| 6) | Herbert CJ, et al. (1988) The NAM2 proteins from S. cerevisiae and S. douglasii are mitochondrial leucyl-tRNA synthetases, and are involved in mRNA splicing. EMBO J 7(2):473-83 |
| 7) | Delarue M (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55 |
| 8) | Arnez JG and Moras D (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6 |
| 9) | 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 |





