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IARS2  -  isoleucyl-tRNA synthetase 2, mitochondrial

Homo sapiens

Synonyms: CAGSSS, FLJ10326, ILERS, IleRS, Isoleucine--tRNA ligase, mitochondrial, ...
 
 
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High impact information on IARS2

  • Single atom substitutions at the 2'- and 3'-hydroxyls of a variety of mischarged RNAs revealed that, while acylation is at the 2'-OH for both enzymes, IleRS catalyzes deacylation specifically from the 3'-OH and not from the 2'-OH [1].
  • RNA minihelices comprised of just the acceptor-TPsiC helix of tRNAIle are substrates for specific aminoacylation by IleRS [2].
  • Accurate discrimination of the structurally similar amino acids, valine and isoleucine, by isoleucyl-tRNA synthetase (IleRS) results, in part, from a hydrolytic editing reaction, which prevents misactivated valine from being stably joined to tRNAIle [2].
  • Isoleucyl-tRNA synthetase (IleRS) catalyzes transfer of isoleucine from the enzyme-bound Ile-AMP and Ile-tRNA to the thiol group of coenzyme A, forming a thioester, Ile-S-CoA [3].
  • Pantetheine also serves as an amino acid acceptor in reactions catalyzed by AspRS, IleRS, and MetRS, forming corresponding aminoacyl-S-pantetheine thioesters [3].

References

  1. Plasticity of recognition of the 3'-end of mischarged tRNA by class I aminoacyl-tRNA synthetases. Nordin, B.E., Schimmel, P. J. Biol. Chem. (2002) [Pubmed]
  2. RNA determinants for translational editing. Mischarging a minihelix substrate by a tRNA synthetase. Nordin, B.E., Schimmel, P. J. Biol. Chem. (1999) [Pubmed]
  3. Aminoacylation of coenzyme A and pantetheine by aminoacyl-tRNA synthetases: possible link between noncoded and coded peptide synthesis. Jakubowski, H. Biochemistry (1998) [Pubmed]
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