Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea.

ABSTRACT: Tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNA^Phe In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. We have suggested previously that a peculiar methyltransferase (aTrm5a/Taw22) likely catalyzes two distinct reactions: N¹-methylation of guanosine to yield m¹G; and C⁷-methylation of imG-14 to yield imG2. Here we show that the recombinant aTrm5a/Taw22-like enzymes from both Pyrococcus abyssi and Nanoarchaeum equitans indeed possess such dual specificity. We also show that substitutions of individual conservative amino acids of P. abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m¹G/imG

SUBMITTER: Urbonavicius J 

PROVIDER: S-EPMC5113207 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature