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Anticodon G recognition by tRNA synthetases mimics the tRNA core.

ABSTRACT: Ancient mechanisms for nucleotide base recognition in the RNA world are candidates for mimicking by early proteins like tRNA synthetases. In the core of the tRNA, conserved G22 interacts with two internal bases in a complex further stabilized by stacking interactions. This particular tRNA format for G recognition is shown here to be adapted by nine different and even nonhomologous anticodon binding domains (ABDs) of tRNA synthetases, in which amino acid side chains mimic all of the tRNA G22 base interactions. We offer the possibility that mimicking this RNA-based mechanism for guanine recognition is perhaps one of the selective pressures for choosing amino acids for the genetic code.

SUBMITTER: Klipcan L

PROVIDER: S-EPMC3634914 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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Anticodon G recognition by tRNA synthetases mimics the tRNA core.

Klipcan Liron L Safro Mark M Schimmel Paul P

Trends in biochemical sciences 20121219 5

Ancient mechanisms for nucleotide base recognition in the RNA world are candidates for mimicking by early proteins like tRNA synthetases. In the core of the tRNA, conserved G22 interacts with two internal bases in a complex further stabilized by stacking interactions. This particular tRNA format for G recognition is shown here to be adapted by nine different and even nonhomologous anticodon binding domains (ABDs) of tRNA synthetases, in which amino acid side chains mimic all of the tRNA G22 base ...[more]

PMID: 23266103

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