| Article ID | Journal | Published Year | Pages | File Type | 
|---|---|---|---|---|
| 10872720 | FEBS Letters | 2005 | 5 Pages | 
Abstract
												There are two oligomeric types of glycyl-tRNA synthetases (GlyRSs) in genome, the α2β2 tetramer and α2 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.
											Keywords
												
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											Authors
												Su-Ni Tang, Jing-Fei Huang, 
											