An insight into the origin and functional evolution of bacterial aromatic ring-hydroxylating oxygenases.
Bacterial aromatic ring-hydroxylating oxygenases (RHOs) are multicomponent enzyme systems which have potential utility in bioremediation of aromatic compounds in the environment. To cope with the enormous diversity of aromatic compounds in the environment, this enzyme family has evolved remarkably exhibiting broad substrate specificity. RHOs are multicomponent enzymes comprising of a homo- or hetero-multimeric terminal oxygenase and one or more electron transport (ET) protein(s). The present study attempts in depicting the evolutionary scenarios that might have occurred during the evolution of RHOs, by analyzing a set of available sequences including those obtained from complete genomes. A modified classification scheme identifying four new RHO types has been suggested on the basis of their evolutionary and functional behaviours, in relation to structural configuration of substrates and preferred oxygenation site(s). The present scheme emphasizes on the fact that the phylogenetic affiliation of RHOs is distributed among four distinct 'Similarity classes', independent of the constituent ET components. Similar combination of RHO components that was previously considered to be equivalent and classified together [Kweon et al., BMC Biochemistry 9, 11 (2008)] were found here in distinct similarity classes indicating the role of substrate-binding terminal oxygenase in guiding the evolution of RHOs irrespective of the nature of constituent ET components. Finally, a model for evolution of the multicomponent RHO enzyme system has been proposed, beginning from genesis of the terminal oxygenase components followed by recruitment of constituent ET components, finally evolving into various 'extant' RHO types.
Department of Microbiology, Bose Institute, Kolkata, 700 054, India.
Joydeep
J
Chakraborty
Debajyoti
D
Ghosal
Arindam
A
Dutta
Tapan K
TK
Dutta
D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology / Q000235:genetics*; D001673:Biodegradation, Environmental; D019143:Evolution, Molecular; D006900:Hydroxylation; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D010105:Oxygenases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D055503:Protein Multimerization; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity
D007506:Iron-Sulfur Proteins; D021122:Protein Subunits; D010105:Oxygenases