MARS (gene)
Methionyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the MARS gene.[1][2]
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene belongs to the class I family of tRNA synthetases.[2]
References
References
- ↑ Ubeda M, Schmitt-Ney M, Ferrer J, Habener JF (Sep 1999). “CHOP/GADD153 and methionyl-tRNA synthetase (MetRS) genes overlap in a conserved region that controls mRNA stability”. Biochem Biophys Res Commun. 262 (1): 31–8. doi:10.1006/bbrc.1999.1140. PMID 10448063.
- ↑ 2.0 2.1 “Entrez Gene: MARS methionyl-tRNA synthetase”.
Further reading
Further reading
- Norcum MT (1991). “Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents”. J. Biol. Chem. 266 (23): 15398–405. PMID 1651330.
- Ogata K, Kurahashi A, Kenmochi N, Terao K (1992). “Role of 5SrRNA as a positive effector of some aminoacyl-tRNA synthetases in macromolecular complexes, with specific reference to methionyl-tRNA synthetase”. J. Biochem. 110 (6): 1037–44. PMID 1665486.
- Cirullo RE, Wasmuth JJ (1984). “Assignment of the human MARS gene, encoding methioninyl-tRNA synthetase, to chromosome 12 using human X Chinese hamster cell hybrids”. Somat. Cell Mol. Genet. 10 (3): 225–34. doi:10.1007/BF01535245. PMID 6585969.
- Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Lage H, Dietel M (1996). “Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase”. Gene. 178 (1–2): 187–9. doi:10.1016/0378-1119(96)00313-7. PMID 8921912.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Quevillon S, Robinson JC, Berthonneau E, et al. (1999). “Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein”. J. Mol. Biol. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.
- Ko YG, Kang YS, Kim EK, et al. (2000). “Nucleolar Localization of Human Methionyl–Trna Synthetase and Its Role in Ribosomal RNA Synthesis”. J. Cell Biol. 149 (3): 567–74. doi:10.1083/jcb.149.3.567. PMC 2174846. PMID 10791971.
- Kang J, Kim T, Ko YG, et al. (2000). “Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases”. J. Biol. Chem. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161.
- Kaminska M, Shalak V, Mirande M (2002). “The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function”. Biochemistry. 40 (47): 14309–16. doi:10.1021/bi015670b. PMID 11714285.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ahn HC, Kim S, Lee BJ (2003). “Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43”. FEBS Lett. 542 (1–3): 119–24. doi:10.1016/S0014-5793(03)00362-4. PMID 12729910.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Ewing RM, Chu P, Elisma F, et al. (2007). “Large-scale mapping of human protein–protein interactions by mass spectrometry”. Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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