gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Tyrosyl-tRNA synthetase 2, mitochondrial

This gene encodes a mitochondrial protein that catalyzes the attachment of tyrosine to tRNA(Tyr). Mutations in this gene are associated with myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2). [provided by RefSeq, Jan 2011] (from NCBI)
Top mentioned proteins: CAN, HAD, ND6, TFAM, SLC25A38
Papers on MtTyrRS
The exome sequencing identified the mutation in YARS2 encoding the mitochondrial tyrosyl-tRNA synthetase as a nuclear modifier for the phenotypic manifestation of Leber's hereditary optic neuropathy-associated mitochondrial DNA mutation.
Guan et al., Hangzhou, China. In Hum Mol Genet, Jan 2016
By using an exome sequencing approach, we identified a LHON susceptibility allele (c.572G>T, p.191Gly>Val) in YARS2 gene encoding mitochondrial tyrosyl-tRNA synthetase, which interacts with m.11778G>A mutation to cause visual failure.
Identification of an anti-TB compound targeting the tyrosyl-tRNA synthetase.
Si et al., Beijing, China. In J Antimicrob Chemother, Aug 2015
This study aimed to identify a new anti-TB agent targeting M. tuberculosis TyrRS (MtTyrRS).
A Novel Homozygous YARS2 Mutation in Two Italian Siblings and a Review of Literature.
Uziel et al., Milano, Italy. In Jimd Rep, 2014
YARS2 encodes the mitochondrial tyrosyl-tRNA synthetase that catalyzes the covalent binding of tyrosine to its cognate mt-tRNA.
Structural states of the flexible catalytic loop of M. tuberculosis tyrosyl-tRNA synthetase in different enzyme-substrate complexes.
Kornelyuk et al., Kiev, Ukraine. In Eur Biophys J, 2014
Tyrosyl-tRNA synthetase from Mycobacterium tuberculosis (MtTyrRS) is an enzyme that belongs to class I of aminoacyl-tRNA synthetases, which catalyze the attachment of L-tyrosine to its cognate tRNATyr in the preribosomal step of protein synthesis.
Mitochondrial myopathy, lactic acidosis, and sideroblastic anemia (MLASA) plus associated with a novel de novo mutation (m.8969G>A) in the mitochondrial encoded ATP6 gene.
Scaglia et al., Houston, United States. In Mol Genet Metab, 2014
Mitochondrial myopathy, lactic acidosis and sideroblastic anemia (MLASA) is a rare mitochondrial disorder that has previously been associated with mutations in PUS1 and YARS2.
A novel homozygous YARS2 mutation causes severe myopathy, lactic acidosis, and sideroblastic anemia 2.
Miyake et al., Yokohama, Japan. In J Hum Genet, 2014
Biallelic mutations in the YARS2 gene encoding mitochondrial tyrosyl-tRNA synthetase cause myopathy, lactic acidosis, and sideroblastic anemia 2 (MLASA2), a type of mitochondrial disease.
Pathophysiology and genetic mutations in congenital sideroblastic anemia.
Harigae et al., Sendai, Japan. In Pediatr Int, 2013
Other known etiologies include mutations in the erythroid specific mitochondrial transporter (SLC25A38), adenosine triphosphate (ATP) binding cassette B7 (ABCB7), glutaredoxin 5 (GLRX5), thiamine transporter SLC19A2, the RNA-modifying enzyme pseudouridine synthase (PUS1), and mitochondrial tyrosyl-tRNA synthase (YARS2), as well as mitochondrial DNA deletions.
A distinct mitochondrial myopathy, lactic acidosis and sideroblastic anemia (MLASA) phenotype associates with YARS2 mutations.
Rahman et al., London, United Kingdom. In Am J Med Genet A, 2013
Clinical diagnosis of MLASA prompted direct sequence analysis of the YARS2 gene encoding the mitochondrial tyrosyl-tRNA synthetase, which revealed homozygosity for a known pathogenic mutation, c.156C>G;p.F52L.
Phenotypic variability and identification of novel YARS2 mutations in YARS2 mitochondrial myopathy, lactic acidosis and sideroblastic anaemia.
Christodoulou et al., Sydney, Australia. In Orphanet J Rare Dis, 2012
BACKGROUND: Mutations in the mitochondrial tyrosyl-tRNA synthetase (YARS2) gene have previously been identified as a cause of the tissue specific mitochondrial respiratory chain (RC) disorder, Myopathy, Lactic Acidosis, Sideroblastic Anaemia (MLASA).
A novel mutation in YARS2 causes myopathy with lactic acidosis and sideroblastic anemia.
Shoubridge et al., Montréal, Canada. In Hum Mutat, 2012
Here, we report a novel missense mutation (c.137G>A, p.Gly46Asp) in the catalytic domain of YARS2, which codes for the mitochondrial tyrosyl-tRNA synthetase, in a subject with myopathy, lactic acidosis, and sideroblastic anemia (MLASA).
Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome.
Christodoulou et al., Sydney, Australia. In Am J Hum Genet, 2010
The YARS2 mutation reported here is an alternative cause of MLASA.
[A model of three-dimensional structure of Mycobacterium tuberculosis tyrosyl-tRNA synthetase].
Korneliuk et al., In Ukr Biokhim Zh (1999), 2008
In this regard, tyrosyl-tRNA synthetase from M. tuberculosis (MtTyrRS) is one of especially attractive target due to its key role in cell metabolism and significant differences between spatial structures of eubacterial and human TyrRSs.
Plasma membrane proteomics of human embryonic stem cells and human embryonal carcinoma cells.
Krijgsveld et al., Utrecht, Netherlands. In J Proteome Res, 2008
These included GAPDH, LDHB, YARS2, CLSTN3, CSDA, LRP6, NDUFA9, and NOL1, which are known to be upregulated in testicular cancer.
Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features.
Rudinger-Thirion et al., Strasbourg, France. In Structure, 2007
the structure of a strictly mitochondrial human synthetase, namely tyrosyl-tRNA synthetase (mt-TyrRS), in complex with an adenylate analog at 2.2 A resolution
Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns.
Platzer et al., Jena, Germany. In Genome Biol, 2006
the apparent occurrence of an unusual TG 3' splice site in intron 5 is discussed
Human mitochondrial TyrRS disobeys the tyrosine identity rules.
Rudinger-Thirion et al., Strasbourg, France. In Rna, 2005
first example of a TyrRS lacking specificity toward N1-N72 and thus of a TyrRS disobeying the identity rules
Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS.
Sissler et al., Strasbourg, France. In Biochemistry, 2005
The gene for mitochondrial tyrosyl-tRNA synthetase is described and the initial characterization of the enzyme is reported. Genes for the remaining missing synthetases have also been found with the exception of human glutaminyl-tRNA synthetase.
share on facebooktweetadd +1mail to friends