Abstract
Protein synthesis is essential for life and requires the correct pairing of amino acids to their cognate transfer RNA (tRNA). Two routes exist to attach asparagine (Asn), to tRNAAsn: the direct and the indirect pathways. The direct path uses asparaginyl-tRNA synthetase to attach Asn to tRNAAsn when free Asn is present. The second pathway involves two steps in which a non-discriminating AspRS attaches aspartate (Asp) to tRNAAsn. The Asp-tRNAAsn is then amidated to Asn by GatCAB. The causative agent for anthrax, Bacillus anthracis, appears to encode both routes for Asn-tRNAAsn formation along with multiple Asn synthetic pathways and two AspRS enzymes. We demonstrate the B. anthracis AspRS acquired by horizontal gene transfer from archaea can attach Asp to tRNAAsn consistent with the organism synthesizing Asn on tRNAAsn using the indirect pathway. The acquisition of a second AspRS may enable B. anthracis to directly couple Asn biosynthesis with its use in translation. This work was supported by Skidmore College and the National Science Foundation (MCB-1244326).
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