A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia

Santosh Kumar Kuncha, Mohd Mazeed, Raghvendra Singh, Bhavita Kattula, Satya Brata Routh and Rajan Sankaranarayanan ()
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Santosh Kumar Kuncha: CSIR–Centre for Cellular and Molecular Biology
Mohd Mazeed: CSIR–Centre for Cellular and Molecular Biology
Raghvendra Singh: CSIR–Centre for Cellular and Molecular Biology
Bhavita Kattula: CSIR–Centre for Cellular and Molecular Biology
Satya Brata Routh: CSIR–Centre for Cellular and Molecular Biology
Rajan Sankaranarayanan: CSIR–Centre for Cellular and Molecular Biology

Nature Communications, 2018, vol. 9, issue 1, 1-13

Abstract: Abstract D-aminoacyl-tRNA deacylase (DTD), a bacterial/eukaryotic trans-editing factor, removes d-amino acids mischarged on tRNAs and achiral glycine mischarged on tRNAAla. An invariant cross-subunit Gly-cisPro motif forms the mechanistic basis of l-amino acid rejection from the catalytic site. Here, we present the identification of a DTD variant, named ATD (Animalia-specific tRNA deacylase), that harbors a Gly-transPro motif. The cis-to-trans switch causes a “gain of function” through L-chiral selectivity in ATD resulting in the clearing of l-alanine mischarged on tRNAThr(G4•U69) by eukaryotic AlaRS. The proofreading activity of ATD is conserved across diverse classes of phylum Chordata. Animalia genomes enriched in tRNAThr(G4•U69) genes are in strict association with the presence of ATD, underlining the mandatory requirement of a dedicated factor to proofread tRNA misaminoacylation. The study highlights the emergence of ATD during genome expansion as a key event associated with the evolution of Animalia.

Date: 2018
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DOI: 10.1038/s41467-017-02204-w

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