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NAM2  -  leucine--tRNA ligase NAM2

Saccharomyces cerevisiae S288c

Synonyms: L3502.6, LeuRS, Leucine--tRNA ligase, mitochondrial, Leucyl-tRNA synthetase, MSL1, ...
 
 
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Disease relevance of NAM2

 

High impact information on NAM2

  • Dominant mutations in the yeast nuclear gene NAM2 cure the RNA splicing deficiency resulting from the inactivation of the bI4 maturase encoded by the fourth intron of the mitochondrial cytochrome b gene [3].
  • This maturase is required to splice the fourth intron of this gene and to splice the fourth intron of the mitochondrial gene oxi3 encoding cytochrome oxidase subunit I. We have cloned the nuclear gene NAM2, which codes for two overlapping RNAs, 3.2 kb and 3.0 kb long, which are transcribed in the same direction but differ at their 5' ends [3].
  • Inactivation of the NAM2 gene either by transplacement with a deleted copy of the gene, or by disruption, is not lethal to the cell, but leads to the destruction of the mitochondrial genome with the production of 100% cytoplasmic petites [3].
  • NAM2 compensating mutations probably result from point mutations in the structural gene [3].
  • Dominant mutations of the nuclear NAM2 gene are able to compensate for a deficiency of the maturase encoded by the fourth intron of the mitochondrial cytochrome b gene [4].
 

Biological context of NAM2

 

Anatomical context of NAM2

 

Associations of NAM2 with chemical compounds

  • The cytoplasmic LeuRS mRNA levels are induced by amino acid starvation resulting from the addition of aminotriazole [7].
  • However, the mitochondrial LeuRS mRNA levels did increase dramatically upon inhibition of mitochondrial protein synthesis by chloramphenicol or ethidium bromide or in the temperature-sensitive strain leu-5 carrying a mutation in the mitochondrial LeuRS structural gene [7].
 

Physical interactions of NAM2

  • Yeast mitochondrial leucyl-tRNA synthetase (LeuRS) binds to the bI4 intron and collaborates with the bI4 maturase to aid excision of the group I intron [8].
 

Enzymatic interactions of NAM2

  • The cloned MSL1 gene was used to construct a strain in which 1 kb of the coding sequence was deleted and substituted with the yeast LEU2 gene [6].
 

Regulatory relationships of NAM2

  • In each case, interactions with only the LeuRS protein fragment specifically stimulated bI4 intron splicing activity [8].
 

Analytical, diagnostic and therapeutic context of NAM2

References

  1. Purification and characterization of the Saccharomyces cerevisiae mitochondrial leucyl-tRNA synthetase. Zagorski, W., Castaing, B., Herbert, C.J., Labouesse, M., Martin, R., Slonimski, P.P. J. Biol. Chem. (1991) [Pubmed]
  2. A prokaryote and human tRNA synthetase provide an essential RNA splicing function in yeast mitochondria. Houman, F., Rho, S.B., Zhang, J., Shen, X., Wang, C.C., Schimmel, P., Martinis, S.A. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  3. The yeast nuclear gene NAM2 is essential for mitochondrial DNA integrity and can cure a mitochondrial RNA-maturase deficiency. Labouesse, M., Dujardin, G., Slonimski, P.P. Cell (1985) [Pubmed]
  4. Three suppressor mutations which cure a mitochondrial RNA maturase deficiency occur at the same codon in the open reading frame of the nuclear NAM2 gene. Labouesse, M., Herbert, C.J., Dujardin, G., Slonimski, P.P. EMBO J. (1987) [Pubmed]
  5. Divergence of the mitochondrial leucyl tRNA synthetase genes in two closely related yeasts Saccharomyces cerevisiae and Saccharomyces douglasii: a paradigm of incipient evolution. Herbert, C.J., Dujardin, G., Labouesse, M., Slonimski, P.P. Mol. Gen. Genet. (1988) [Pubmed]
  6. Homology of yeast mitochondrial leucyl-tRNA synthetase and isoleucyl- and methionyl-tRNA synthetases of Escherichia coli. Tzagoloff, A., Akai, A., Kurkulos, M., Repetto, B. J. Biol. Chem. (1988) [Pubmed]
  7. Regulation of the nuclear genes encoding the cytoplasmic and mitochondrial leucyl-tRNA synthetases of Neurospora crassa. Chow, C.M., Rajbhandary, U.L. Mol. Cell. Biol. (1989) [Pubmed]
  8. An inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing. Rho, S.B., Lincecum, T.L., Martinis, S.A. EMBO J. (2002) [Pubmed]
  9. Association between Archaeal prolyl- and leucyl-tRNA synthetases enhances tRNA(Pro) aminoacylation. Praetorius-Ibba, M., Rogers, T.E., Samson, R., Kelman, Z., Ibba, M. J. Biol. Chem. (2005) [Pubmed]
 
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