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Discriminating Nature of the B. anthracis Aspartyl‐tRNA Synthetases
Author(s) -
Erskine Julia,
Sheppard Kelly
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.892.8
Subject(s) - transfer rna , bacillus anthracis , asparagine , computational biology , archaea , translation (biology) , direct pathway of movement , biology , enzyme , rna , genetics , biochemistry , gene , bacteria , messenger rna , neuroscience , basal ganglia , central nervous system
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 tRNA Asn : the direct and the indirect pathways. The direct path uses asparaginyl‐tRNA synthetase to attach Asn to tRNA Asn when free Asn is present. The second pathway involves two steps in which a non‐discriminating AspRS attaches aspartate (Asp) to tRNA Asn . The Asp‐tRNA Asn is then amidated to Asn by GatCAB. The causative agent for anthrax, Bacillus anthracis , appears to encode both routes for Asn‐tRNA Asn 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 tRNA Asn consistent with the organism synthesizing Asn on tRNA Asn 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).