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Asparaginyl-tRNA (Asn-tRNA) and glutaminyl-tRNA (Gln-tRNA) are essential components of protein synthesis. They can be formed by direct acylation by asparaginyl-tRNA synthetase (AsnRS) or glutaminyl-tRNA synthetase (GlnRS). The alternative route involves transamidation of incorrectly charged tRNA. Examination of the preliminary genomic sequence of the radiation-resistant bacteriumDeinococcus radiodurans suggests the presence of both direct and indirect routes of Asn-tRNA and Gln-tRNA formation. Biochemical experiments demonstrate the presence of AsnRS and GlnRS, as well as glutamyl-tRNA synthetase (GluRS), a discriminating and a nondiscriminating aspartyl-tRNA synthetase (AspRS). Moreover, both Gln-tRNA and Asn-tRNA transamidation activities are present. Surprisingly, they are catalyzed by a single enzyme encoded by three ORFs orthologous toBacillus subtilis gatCAB . However, the transamidation route to Gln-tRNA formation is idled by the inability of the discriminatingD. radiodurans GluRS to produce the required mischarged Glu-tRNAGln substrate. The presence of apparently redundant complete routes to Asn-tRNA formation, combined with the absence from theD. radiodurans genome of genes encoding tRNA-independent asparagine synthetase and the lack of this enzyme inD. radiodurans extracts, suggests that thegatCAB genes may be responsible for biosynthesis of asparagine in this asparagine prototroph.

Glutamyl-tRNA Gln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis

Glutamyl-tRNA ^Gln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis