Expression of Animalia-specific tRNA deacylase in cell types
Proteins are essential macromolecules of life. The biological information transfer from DNA to proteins via transcription and translation have errors associated with them. Proteins are synthesized by ribosomes with aminoacyl-tRNA as its substrate and mRNA acting as its template. Translational fidelity largely depends on the correctness of amino acid and tRNA, pairing which is done by enzymes called aminoacyl-tRNA synthetases (aaRSs). aaRSs face enormous challenge in choosing the correct amino acid, wherein the differences are as small as a methyl group. As a result, aaRSs mischarge tRNAs with incorrect amino acid which is proofread by editing domains. Recently tRNA mis-selection was identified in kingdom Animalia, in which alanyl-tRNA synthetase (AlaRS) mischarges L-alanine on non-cognate tRNAThr containing G4●U69 (tRNA determinant of AlaRS is G3●U70), as a result L-Ala-tRNAThr is formed which may lead to mis-incorporations of alanine at threonine codons. Recently, a new proofreader which decouples these erroneously mischarged tRNAs, was identified and named as Animalia-specific tRNA deacylase (ATD). However, the physiological relevance of ATD is still unknown. My work involved checking the expression levels of ATD in different cell types using western blot analysis.
Keywords: proofreader, aminoacyl-tRNA synthetases, Animalia-specific tRNA deacylase