title: Evolution of different oligomeric glycyl-tRNA synthetases.
abstract: There are two oligomeric types of glycyl-tRNA synthetases (GlyRSs) in genome, the alpha2beta2 tetramer and alpha2 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 alpha-subunit, but the tetrameric GlyRS_ABD is to the C-terminal in beta-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.
authors.affiliation: Key Laboratory of Cellular and Molecular Evolution, Kunming Institute of Zoology, Chinese Academy of Sciences, 32 Eastern Jiaochang Road, Kunming, Yunnan 650223, PR China.
authors.forename: Su-Ni
authors.initials: SN
authors.lastname: Tang
authors.forename: Jing-Fei
authors.initials: JF
authors.lastname: Huang
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D019281:Dimerization; D019143:Evolution, Molecular; D005798:Genes, Bacterial / Q000235:genetics; D016680:Genome, Bacterial; D006032:Glycine-tRNA Ligase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D042201:Magnetospirillum / Q000201:enzymology / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
chemical_list: D006032:Glycine-tRNA Ligase