NAM2/YLR382C Literature Guide Help

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

NAM2 - Strains/Constructs (18)

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
Sarkar J, et al.  (2012) Yeast mitochondrial leucyl-tRNA synthetase CP1 domain has functionally diverged to accommodate RNA splicing at expense of hydrolytic editing. J Biol Chem 287(18):14772-81
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
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
Montanari A, et al.  (2010) Aminoacyl-tRNA synthetases are multivalent suppressors of defects due to human equivalent mutations in yeast mt tRNA genes. Biochim Biophys Acta 1803(9):1050-1057
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
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
De Luca C, et al.  (2006) Mutations in yeast mt tRNAs: specific and general suppression by nuclear encoded tRNA interactors. Gene 377():169-76
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
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.  (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