Evolution of substrate specificity in a retained enzyme driven by gene loss

• DOI: 10.7554/elife.22679
• Publication Date: 2017-03-31T12:08:58Z
• Authors: Ana Lilia Juárez-...; Janaka N Edirisinghe; Ernesto A Verduzc...; Karolina Michalska; Chenggang Wu; Lianet Noda-García; Gyorgy Babnigg; Michael Endres; Sofía Medina-Ruíz; Julián Santoyo-Fl...; Mauricio Carrillo...; Hung Ton-That; Andrzej Joachimiak; Christopher S Henry; Francisco Barona-...
• Keywords: Negative selection

The connection between gene loss and the functional adaptation of retained proteins is still poorly understood. We apply phylogenomics metabolic modeling to detect bacterial species that are evolving by loss, with finding Actinomycetaceae genomes from human cavities undergoing sizable reductions, including L-histidine L-tryptophan biosynthesis. observe dual-substrate phosphoribosyl isomerase A or priA gene, at which these pathways converge, appears coevolve occurrence trp his genes. Characterization a dozen PriA homologs shows enzymes adapt bifunctionality in largest genomes, monofunctional, yet not necessarily specialized, inefficient form reduction. These changes accomplished via mutations, result relaxation purifying selection, residues structurally mapped after sequence X-ray structural analyses. Our results show how can drive evolution substrate specificity enzymes.