NAM2/YLR382C Literature Guide Help

Other names published for NAM2: MSL1, mitochondrial leucyl-tRNA synthetase, LeuRS, leucine--tRNA ligase NAM2, YLR382C

NAM2 - Mutants/Phenotypes (22)

ReferenceOther Genes Addressed
Lanza AM, et al.  (2012) Linking yeast Gcn5p catalytic function and gene regulation using a quantitative, graded dominant mutant approach. PLoS One 7(4):e36193
Francisci S, et al.  (2011) Peptides from aminoacyl-tRNA synthetases can cure the defects due to mutations in mt tRNA genes. Mitochondrion 11(6):919-23
Montanari A, et al.  (2011) Structural and functional role of bases 32 and 33 in the anticodon loop of yeast mitochondrial tRNAIle. RNA 17(11):1983-96
Yadav V, et al.  (2011) Chlorophenol stress affects aromatic amino acid biosynthesis-a genome-wide study. Yeast 28(1):81-91
Banuelos MG, et al.  (2010) Genomic analysis of severe hypersensitivity to hygromycin B reveals linkage to vacuolar defects and new vacuolar gene functions in Saccharomyces cerevisiae. Curr Genet 56(2):121-37
De Luca C, et al.  (2009) Can yeast be used to study mitochondrial diseases? Biolistic tRNA mutants for the analysis of mechanisms and suppressors. Mitochondrion 9(6):408-17
Hsu JL and Martinis SA  (2008) A Flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases. J Mol Biol 376(2):482-91
Fairn GD, et al.  (2007) A chemogenomic screen in Saccharomyces cerevisiae uncovers a primary role for the mitochondria in farnesol toxicity and its regulation by the Pkc1 pathway. J Biol Chem 282(7):4868-74
Nawaz MH, et al.  (2007) Molecular and functional dissection of a putative RNA-binding region in yeast mitochondrial leucyl-tRNA synthetase. J Mol Biol 367(2):384-94
Hsu JL, et al.  (2006) Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles. J Biol Chem 281(32):23075-82
Karkhanis VA, et al.  (2006) A viable amino acid editing activity in the leucyl-tRNA synthetase CP1-splicing domain is not required in the yeast mitochondria. J Biol Chem 281(44):33217-25
Rand JD and Grant CM  (2006) The thioredoxin system protects ribosomes against stress-induced aggregation. Mol Biol Cell 17(1):387-401
Dimmer KS, et al.  (2002) Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell 13(3):847-53
Rho SB, et al.  (2002) An inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing. EMBO J 21(24):6874-81
Houman F, et al.  (2000) A prokaryote and human tRNA synthetase provide an essential RNA splicing function in yeast mitochondria. Proc Natl Acad Sci U S A 97(25):13743-8
Li GY, et al.  (1996) In vitro mutagenesis of the mitochondrial leucyl tRNA synthetase of Saccharomyces cerevisiae shows that the suppressor activity of the mutant proteins is related to the splicing function of the wild-type protein. Mol Gen Genet 252(6):667-75
Li GY, et al.  (1992) In vitro mutagenesis of the mitochondrial leucyl-tRNA synthetase of S. cerevisiae reveals residues critical for its in vivo activities. Curr Genet 22(1):69-74
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
Tzagoloff A, et al.  (1988) Homology of yeast mitochondrial leucyl-tRNA synthetase and isoleucyl- and methionyl-tRNA synthetases of Escherichia coli. J Biol Chem 263(2):850-6
Labouesse M, et al.  (1987) 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. EMBO J 6(3):713-21
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
Groudinsky O, et al.  (1981) Long range control circuits within mitochondria and between nucleus and mitochondria. II. Genetic and biochemical analyses of suppressors which selectively alleviate the mitochondrial intron mutations. Mol Gen Genet 184(3):493-503