Abstract
The identity of the histidine specific transfer RNA (tRNA His) is largely determined by a unique guanosine residue at position −1. In eukaryotes and archaea, the tRNA His guanylyltransferase (Thg1) catalyzes 3′–5′ addition of G to the 5′-terminus of tRNA His. Here, we show that Thg1 also occurs in bacteria. We demonstrate in vitro Thg1 activity for recombinant enzymes from the two bacteria Bacillus thuringiensis and Myxococcus xanthus and provide a closer investigation of several archaeal Thg1. The reaction mechanism of prokaryotic Thg1 differs from eukaryotic enzymes, as it does not require ATP. Complementation of a yeast thg1 knockout strain with bacterial Thg1 verified in vivo activity and suggests a relaxed recognition of the discriminator base in bacteria.
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