Recurrent intragenomic recombination leading to sequence homogenization during the evolution of the lipoyl-binding domain.
The lipoyl-binding domain is often present, in one or several copies, in the E2 subunit and, less often, in the E1 and E3 subunits of 2-oxo acid dehydrogenase complexes. Phylogenetic analysis shows evidence of multiple, independent intragenomic recombination events between different versions of the lipoyl-binding domain in various bacteria and eukaryotic mitochondria, leading to homogenization of the sequences of the lipoyl-binding domain within the same enzymatic complex in several bacterial lineages. This appears to be the first case of sequence homogenization at the level of an individual domain in prokaryotes.
Omelchenko
Marina V
MV
Department of Pathology, F.E. Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD 20814-4799, USA.
Makarova
Kira S
KS
Koonin
Eugene V
EV
D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D001419:Bacteria / Q000201:enzymology / Q000235:genetics*; D019143:Evolution, Molecular; D020440:Gene Duplication; D007658:Ketone Oxidoreductases / Q000737:chemistry* / Q000235:genetics*; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000235:genetics*; D010802:Phylogeny; D011995:Recombination, Genetic / Q000235:genetics*
D009097:Multienzyme Complexes; D007658:Ketone Oxidoreductases; D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)