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Dual Routes for B. subtilis Asparaginyl‐tRNA Formation
Author(s) -
Raff Hannah,
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.892.9
Subject(s) - transfer rna , bacillus subtilis , asparagine , organism , threonine , protein biosynthesis , biochemistry , computational biology , biology , biosynthesis , glutamine amidotransferase , rna , glutamine , genetics , enzyme , amino acid , bacteria , gene , serine
Two distinct routes for attaching asparagine (Asn) to its cognate transfer RNA (tRNA Asn ), an essential step in protein synthesis, are known. The one‐step, direct pathway uses an asparaginyl‐tRNA synthetase (AsnRS) to aminoacylate Asn to tRNA Asn . In organisms lacking AsnRS, a two‐step pathway is used. First a non‐discriminating aspartyl‐tRNA synthetase (ND‐AspRS) attaches aspartate (Asp) to tRNA Asn . The Asp is then amidated to Asn by GatCAB. Despite Bacillus subtilis using AsnRS for Asn‐tRNA Asn production and GatCAB for Gln‐tRNA Gln formation, we predicted the lone B. subtilis AspRS is non‐discriminating to enable the organism to also use the two‐step pathway for Asn‐tRNA Asn formation. Our in vitro and in vivo results are consistent with the AspRS using tRNA Asn as a substrate as the first step in tRNA‐dependent Asn biosynthesis. B. subtilis encoding a tRNA‐dependent route for Asn production would explain why the organism is able to grow in the absence Asn when all three of its glutamine‐dependent Asn synthetases are knocked out. This work was supported by Skidmore College and the National Science Foundation (MCB‐1244326)