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10.7554/eLife.22679 http://scihub22266oqcxt.onion/10.7554/eLife.22679 C5404923!5404923!28362260     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28362260&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2017 ; 6 (ä): ä Nephropedia Template TP {{tp|p=28362260|t=2017. Evolution of substrate specificity in a retained enzyme driven by gene loss |pdf=|usr=}}{{28362260}} gab.com Text Evolution of substrate specificity in a retained enzyme driven by gene loss JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=28362260 #FOAvip 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.DOI:http://dx.doi.org/10.7554/eLife.22679.001 Twit Text FOAVip Evolution of substrate specificity in a retained enzyme driven by gene loss ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=28362260 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28362260 #FOAvip English Wikipedia <ref>{{Cite pmid|28362260}}</ref> Evolution of substrate specificity in a retained enzyme driven by gene loss #MMPMID28362260 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 F eLife 2017[]; 6 (ä): ä PMID28362260show ga 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.DOI:http://dx.doi.org/10.7554/eLife.22679.001 äEvolution of substrate specificity in a retained enzyme driven by gene(epmc).pdf DeepDyve Pubget Overpricing