Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/40574
metadata.artigo.dc.title: Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes
metadata.artigo.dc.creator: Cruz, Dennifier Costa Brandão
Santana, Lenon Lima
Guedes, Alexandre Siqueira
Souza, Jorge Teodoro de
Marbach, Phellippe Arthur Santos
metadata.artigo.dc.subject: Archaea
Bacteria
Bioinformatics
Comparative genomics
Evolution
Phylogeny
Procariontes
Bioinformática
Genômica comparativa
Evolução
Filogenia
metadata.artigo.dc.publisher: Oxford University Press
metadata.artigo.dc.date.issued: 2019
metadata.artigo.dc.identifier.citation: CRUZ, 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.
metadata.artigo.dc.description.abstract: The 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.
metadata.artigo.dc.identifier.uri: http://repositorio.ufla.br/jspui/handle/1/40574
metadata.artigo.dc.language: en
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