Abstract:
:The connection between gene loss and the functional adaptation of retained proteins is still poorly understood. We apply phylogenomics and metabolic modeling to detect bacterial species that are evolving by gene loss, with the finding that Actinomycetaceae genomes from human cavities are undergoing sizable reductions, including loss of L-histidine and L-tryptophan biosynthesis. We observe that the dual-substrate phosphoribosyl isomerase A or priA gene, at which these pathways converge, appears to coevolve with the occurrence of trp and his genes. Characterization of a dozen PriA homologs shows that these enzymes adapt from bifunctionality in the largest genomes, to a monofunctional, yet not necessarily specialized, inefficient form in genomes undergoing reduction. These functional changes are accomplished via mutations, which result from relaxation of purifying selection, in residues structurally mapped after sequence and X-ray structural analyses. Our results show how gene loss can drive the evolution of substrate specificity from retained enzymes.
journal_name
Elifejournal_title
eLifeauthors
Juárez-Vázquez AL,Edirisinghe JN,Verduzco-Castro EA,Michalska K,Wu C,Noda-García L,Babnigg G,Endres M,Medina-Ruíz S,Santoyo-Flores J,Carrillo-Tripp M,Ton-That H,Joachimiak A,Henry CS,Barona-Gómez Fdoi
10.7554/eLife.22679subject
Has Abstractpub_date
2017-03-31 00:00:00issn
2050-084Xjournal_volume
6pub_type
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