1887

Abstract

Only about half of bacterial species use an asparaginyl-tRNA synthetase (AsnRS) to attach Asn to its cognate tRNA. Other bacteria, including the human pathogen , a causative agent of otitis media, lack a gene encoding AsnRS, and form Asn-tRNA by an indirect pathway catalysed by two enzymes: first, a non-discriminating aspartyl-tRNA synthetase (ND-AspRS) catalyses the formation of aspartyl-tRNA (Asp-tRNA); then, a tRNA-dependent amidotransferase (GatCAB) transamidates this ‘incorrect’ product into Asn-tRNA. As has a Gln-tRNA synthetase, its GatCAB functions as an Asp-tRNA amidotransferase. This pathogen rapidly evolved to about 90 % ampicillin resistance worldwide by insertion of a β-lactamase gene within the operon. Comparison of the GatCAB subunits from β-lactamase-positive and -negative strains showed that the laterally transferred gene, inserted into the operon, affected the C-terminal sequence of GatA. The identity between the C-terminal sequences of GatA (residues 479–491) and of GatA (residues 479–492) was about 36 %, whereas the rest of the GatA sequence was relatively conserved. The characterization of these two distinct GatCABs as well as the hybrid GatCAB containing GatA(1–478)(479–492) and truncated GatCAB enzymes of showed that the substitution in GatA of residues 479–492 of GatA causes increased specificity for glutamine, and decreased specificity for Asp-tRNA in the transamidation reaction. We conclude that the gene insertion has altered the kinetic parameters of Asp-tRNA amidotransferase, and we propose a model for evolution after the insertion of at the carboxyl end of .

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2012-09-01
2019-10-21
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