When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism.

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Roy H, Becker HD, Reinbolt J, Kern D

When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism.

Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9837-42. Epub 2003 Jul 21.

PubMed ID

12874385 [ View in PubMed

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Abstract

Faithful protein synthesis relies on a family of essential enzymes called aminoacyl-tRNA synthetases, assembled in a piecewise fashion. Analysis of the completed archaeal genomes reveals that all archaea that possess asparaginyl-tRNA synthetase (AsnRS) also display a second ORF encoding an AsnRS truncated from its anticodon binding-domain (AsnRS2). We show herein that Pyrococcus abyssi AsnRS2, in contrast to AsnRS, does not sustain asparaginyl-tRNAAsn synthesis but is instead capable of converting aspartic acid into asparagine. Functional analysis and complementation of an Escherichia coli asparagine auxotrophic strain show that AsnRS2 constitutes the archaeal homologue of the bacterial ammonia-dependent asparagine synthetase A (AS-A), therefore named archaeal asparagine synthetase A (AS-AR). Primary sequence- and 3D-based phylogeny shows that an archaeal AspRS ancestor originated AS-AR, which was subsequently transferred into bacteria by lateral gene transfer in which it underwent structural changes producing AS-A. This study provides evidence that a contemporary aminoacyl-tRNA synthetase can be recruited to sustain amino acid metabolism.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Asparagine	Probable asparagine--tRNA ligase, mitochondrial	Protein	Humans	Unknown	Not Available	Details