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dc.creatorCruz, Dennifier Costa Brandão-
dc.creatorSantana, Lenon Lima-
dc.creatorGuedes, Alexandre Siqueira-
dc.creatorSouza, Jorge Teodoro de-
dc.creatorMarbach, Phellippe Arthur Santos-
dc.date.accessioned2020-05-05T12:42:14Z-
dc.date.available2020-05-05T12:42:14Z-
dc.date.issued2019-
dc.identifier.citationCRUZ, D. C. B. et al. Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes. Genome Biology and Evolution, Oxford, v. 11, n. 4, p. 1235-1249, Apr. 2019.pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/40574-
dc.description.abstractThe last two steps of the purine biosynthetic pathway may be catalyzed by different enzymes in prokaryotes. The genes that encode these enzymes include homologs of purH, purP, purO and those encoding the AICARFT and IMPCH domains of PurH, here named purV and purJ, respectively. In Bacteria, these reactions are mainly catalyzed by the domains AICARFT and IMPCH of PurH. In Archaea, these reactions may be carried out by PurH and also by PurP and PurO, both considered signatures of this domain and analogous to the AICARFT and IMPCH domains of PurH, respectively. These genes were searched for in 1,403 completely sequenced prokaryotic genomes publicly available. Our analyses revealed taxonomic patterns for the distribution of these genes and anticorrelations in their occurrence. The analyses of bacterial genomes revealed the existence of genes coding for PurV, PurJ, and PurO, which may no longer be considered signatures of the domain Archaea. Although highly divergent, the PurOs of Archaea and Bacteria show a high level of conservation in the amino acids of the active sites of the protein, allowing us to infer that these enzymes are analogs. Based on the results, we propose that the gene purO was present in the common ancestor of all living beings, whereas the gene encoding PurP emerged after the divergence of Archaea and Bacteria and their isoforms originated in duplication events in the common ancestor of phyla Crenarchaeota and Euryarchaeota. The results reported here expand our understanding of the diversity and evolution of the last two steps of the purine biosynthetic pathway in prokaryotes.pt_BR
dc.languageenpt_BR
dc.publisherOxford University Presspt_BR
dc.rightsacesso abertopt_BR
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/*
dc.sourceGenome Biology and Evolutionpt_BR
dc.subjectArchaeapt_BR
dc.subjectBacteriapt_BR
dc.subjectBioinformaticspt_BR
dc.subjectComparative genomicspt_BR
dc.subjectEvolutionpt_BR
dc.subjectPhylogenypt_BR
dc.subjectProcariontespt_BR
dc.subjectBioinformáticapt_BR
dc.subjectGenômica comparativapt_BR
dc.subjectEvoluçãopt_BR
dc.subjectFilogeniapt_BR
dc.titleDifferent ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotespt_BR
dc.typeArtigopt_BR
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