Evolution of different oligomeric glycyl-tRNA synthetases

Abstract

There are two oligomeric types of glycyl-tRNA synthetases (GlyRSs) in genome, the α 2β 2 tetramer and α 2 dimer. Here, we showed that the anticodon-binding domains (ABDs) of dimeric and tetrameric GlyRSs are non-homologous, although their catalytic central domains (CCDs) are homologous. The dimeric GlyRS_ABD is fused to the C-terminal of CCD in α-subunit, but the tetrameric GlyRS_ABD is to the C-terminal in β-subunit during evolution. Generally, one species only contains one oligomeric type of GlyRS, but the both oligomeric GlyRSs with the multiple homologous domains can be observed in Magnetospirillum magnetotacticum genome, nevertheless, these homologous domains are probably from different genomes.