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Alanyl-tRNA synthetase

alanyl-tRNA synthetase, Alanine-tRNA Ligase
The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41% identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: ACID, CAN, HAD, 5-aminolevulinate synthase, Phosphogluconate Dehydrogenase
Papers on alanyl-tRNA synthetase
Genotype/phenotype correlations in AARS-related neuropathy in a cohort of patients from the United Kingdom and Ireland.
Horvath et al., Newcastle upon Tyne, United Kingdom. In J Neurol, Aug 2015
To date six families have been reported worldwide with dominant missense alanyl-tRNA synthetase (AARS) mutations leading to clinically heterogeneous axonal neuropathies.
A novel AARS mutation in a family with dominant myeloneuropathy.
Scherer et al., Antwerp, Belgium. In Neurology, Jun 2015
All affected family members had a heterozygous missense mutation c.304G>C (p.Gly102Arg) in the alanyl-tRNA synthetase (AARS) gene; this allele was not identified in unaffected individuals or control samples.
Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation.
Musier-Forsyth et al., Tokyo, Japan. In Proc Natl Acad Sci U S A, Jun 2015
Taken together, our data suggest that these free-standing editing domains have the ability to prevent mistranslation errors caused by a number of ARSs, including lysyl-tRNA synthetase, threonyl-tRNA synthetase, seryl-tRNA synthetase, and alanyl-tRNA synthetase.
Urea Unfolding Study of E. coli Alanyl-tRNA Synthetase and Its Monomeric Variants Proves the Role of C-Terminal Domain in Stability.
Banerjee et al., Calcutta, India. In J Amino Acids, 2014
Urea induced denaturation of these monomeric mutants along with another alaRS variant (N461 alaRS) was studied together with the full-length enzyme using various spectroscopic techniques such as intrinsic tryptophan fluorescence, 1-anilino-8-naphthalene-sulfonic acid binding, near- and far-UV circular dichroism, and analytical ultracentrifugation.
Non-Conserved Residues in Clostridium acetobutylicum tRNA(Ala) Contribute to tRNA Tuning for Efficient Antitermination of the alaS T Box Riboswitch.
Henkin et al., Columbus, United States. In Life (basel), 2014
In this study, we used the Clostridium acetobutylicum alaS gene, which encodes alanyl-tRNA synthetase, to investigate the specificity of the tRNA response.
The selective tRNA aminoacylation mechanism based on a single G•U pair.
Yokoyama et al., Yokohama, Japan. In Nature, 2014
Throughout evolution, tRNA(Ala) selection by alanyl-tRNA synthetase (AlaRS) has depended predominantly on a single wobble base pair in the acceptor stem, G3•U70, mainly on the kcat level.
Alanyl-tRNA synthetase mutation in a family with dominant distal hereditary motor neuropathy.
Takashima et al., Shijiazhuang, China. In Neurology, 2012
in a family with distal hereditary motor neuropathy (dHMN), all 4 affected family members had a heterozygous missense mutation c.2677G>A (p.D893N) of (AARS), not found in the 4 unaffected members and control subjects; conclude AARS mutation caused dHMN in a Chinese family; AARS mutations result in not only a CMT phenotype but also a dHMN phenotype
A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N).
Antonellis et al., Ann Arbor, United States. In Hum Mutat, 2012
Methylation-mediated deamination of a CpG dinucleotide gives rise to the recurrent p.Arg329His alanyl-tRNA synthetase mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N).
Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy.
Suomalainen et al., Helsinki, Finland. In Am J Hum Genet, 2011
We show here that mutations in AARS2 cause perinatal or infantile cardiomyopathy with near-total combined mitochondrial respiratory chain deficiency in the heart.
A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease.
Rousson et al., Bron, France. In Am J Hum Genet, 2010
cytoplasmic Alanyl-tRNA synthetase may have a role in dominant axonal Charcot-Marie-Tooth disease, as shown by its mutation in a major determinant for binding and aminoacylation
Distinct domains of tRNA synthetase recognize the same base pair.
Schimmel et al., Los Angeles, United States. In Nature, 2008
A single specific G.U base pair (G3.U70) marks a tRNA for aminoacylation by alanyl-tRNA synthetase.
Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration.
Ackerman et al., Bar Harbor, United States. In Nature, 2006
We report that the mouse sticky mutation, which causes cerebellar Purkinje cell loss and ataxia, is a missense mutation in the editing domain of the alanyl-tRNA synthetase gene that compromises the proofreading activity of this enzyme during aminoacylation of tRNAs.
Protein signatures distinctive of alpha proteobacteria and its subgroups and a model for alpha-proteobacterial evolution.
Gupta, Hamilton, Canada. In Crit Rev Microbiol, 2004
The signatures in succinyl-CoA synthetase, cytochrome oxidase I, alanyl-tRNA synthetase, and MutS proteins are found in all alpha-proteobacteria, except the Rickettsiales, indicating that this group has diverged prior to the introduction of these signatures.
Emerging views on tmRNA-mediated protein tagging and ribosome rescue.
Felden et al., Rennes, France. In Mol Microbiol, 2001
tmRNA acts initially as transfer RNA (tRNA), being aminoacylated at its 3'-end by alanyl-tRNA synthetase, to add alanine to the stalled polypeptide chain.
[Analysis of autoantigens and clinical significance of antinuclear antibodies].
Ohosone et al., Tokyo, Japan. In Rinsho Byori, 1998
Two of 15 sera containing anti-tRNA antibodies were identified as anti-PL-12 (alanyl-tRNA synthetase) antibodies.
Functional evidence for indirect recognition of G.U in tRNA(Ala) by alanyl-tRNA synthetase.
McClain et al., Madison, United States. In Science, 1996
The structural features of the G.U wobble pair in Escherichia coli alanine transfer RNA (tRNA(Ala)) that are associated with aminoacylation by alanyl-tRNA synthetase (AlaRS) were investigated in vivo for wild-type tRNA(Ala) and mutant tRNAs with G.U substitutions.
Humoral immunity in polymyositis/dermatomyositis.
Targoff, Oklahoma City, United States. In J Invest Dermatol, 1993
Sera with antibodies to alanyl-tRNA synthetase (anti-PL-12) also have antibodies to tRNA(ala), whereas most sera with other anti-synthetases do not react directly with tRNA.
Polymyositis, pulmonary fibrosis and autoantibodies to aminoacyl-tRNA synthetase enzymes.
Walport et al., London, United Kingdom. In Q J Med, 1990
The clinical and laboratory features of 29 patients who had one of three anti-aminoacyl-tRNA synthetase autoantibodies, anti-Jo1 (histidyl-tRNA synthetase), anti-PL12 (alanyl-tRNA synthetase) or anti-PL7 (threonyl-tRNA synthetase) were analysed and compared with the findings of other published reports.
Autoreactive epitope defined as the anticodon region of alanine transfer RNA.
Mathews et al., Old Harbour, Jamaica. In Science, 1987
Sera of the PL-12 specificity contain separate antibodies reacting with alanyl-tRNA synthetase and alanine tRNA (tRNAAla).
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