Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation.

We suggest that modification selectivity of the Cys 409 site in hmtThrRS was highly significant because this residue has the potential to function as a switch to effectively regulate aminoacylation activity and the corresponding mitochondrial protein synthesis rate in a timely and precise manner, similar to the modification of editing-essential Cys 182 in Ec ThrRS for modulating its proofreading activity and protein mistranslation in E. coli under H 2 O 2 stress ( 31 , 32 ).

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