Abstract
Protein synthesis is essential for life and requires the correct pairing of amino acids to their cognate transfer tRNA (aminoacylation). To date, only two routes exist to attach asparagine (Asn), to it cognate 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 Asn is synthesized by asparagine synthetase A. The second pathway involves synthesizing Asn on the tRNA itself. The causative agent for anthrax, Bacillus anthracis, appears to encode both routes for Asn‐tRNAAsn formation. We would like to understand why B. anthraciscodes for both routes. This semester we have focused on the direct pathway. We report the successful purification of the asparagine synthetase A and asparaginyl‐tRNA synthetase along with activity measurements of asparagine synthetase A in order to characterize the direct pathway under different physiologically relevant conditions.Support or Funding InformationNational Science Foundation (MCB‐1615770)
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