Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFLA |
Texto Completo: | http://repositorio.ufla.br/jspui/handle/1/40574 |
Resumo: | 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. |
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Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotesArchaeaBacteriaBioinformaticsComparative genomicsEvolutionPhylogenyProcariontesBioinformáticaGenômica comparativaEvoluçãoFilogeniaThe 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.Oxford University Press2020-05-05T12:42:14Z2020-05-05T12:42:14Z2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfCRUZ, 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.http://repositorio.ufla.br/jspui/handle/1/40574Genome Biology and Evolutionreponame:Repositório Institucional da UFLAinstname:Universidade Federal de Lavras (UFLA)instacron:UFLAhttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccessCruz, Dennifier Costa BrandãoSantana, Lenon LimaGuedes, Alexandre SiqueiraSouza, Jorge Teodoro deMarbach, Phellippe Arthur Santoseng2023-05-26T19:52:25Zoai:localhost:1/40574Repositório InstitucionalPUBhttp://repositorio.ufla.br/oai/requestnivaldo@ufla.br || repositorio.biblioteca@ufla.bropendoar:2023-05-26T19:52:25Repositório Institucional da UFLA - Universidade Federal de Lavras (UFLA)false |
dc.title.none.fl_str_mv |
Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes |
title |
Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes |
spellingShingle |
Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes Cruz, Dennifier Costa Brandão Archaea Bacteria Bioinformatics Comparative genomics Evolution Phylogeny Procariontes Bioinformática Genômica comparativa Evolução Filogenia |
title_short |
Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes |
title_full |
Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes |
title_fullStr |
Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes |
title_full_unstemmed |
Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes |
title_sort |
Different ways of doing the same: variations in the two last steps of the purine biosynthetic pathway in prokaryotes |
author |
Cruz, Dennifier Costa Brandão |
author_facet |
Cruz, Dennifier Costa Brandão Santana, Lenon Lima Guedes, Alexandre Siqueira Souza, Jorge Teodoro de Marbach, Phellippe Arthur Santos |
author_role |
author |
author2 |
Santana, Lenon Lima Guedes, Alexandre Siqueira Souza, Jorge Teodoro de Marbach, Phellippe Arthur Santos |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Cruz, Dennifier Costa Brandão Santana, Lenon Lima Guedes, Alexandre Siqueira Souza, Jorge Teodoro de Marbach, Phellippe Arthur Santos |
dc.subject.por.fl_str_mv |
Archaea Bacteria Bioinformatics Comparative genomics Evolution Phylogeny Procariontes Bioinformática Genômica comparativa Evolução Filogenia |
topic |
Archaea Bacteria Bioinformatics Comparative genomics Evolution Phylogeny Procariontes Bioinformática Genômica comparativa Evolução Filogenia |
description |
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. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019 2020-05-05T12:42:14Z 2020-05-05T12:42:14Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
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. http://repositorio.ufla.br/jspui/handle/1/40574 |
identifier_str_mv |
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. |
url |
http://repositorio.ufla.br/jspui/handle/1/40574 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
http://creativecommons.org/licenses/by-nc/4.0/ info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc/4.0/ |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Oxford University Press |
publisher.none.fl_str_mv |
Oxford University Press |
dc.source.none.fl_str_mv |
Genome Biology and Evolution reponame:Repositório Institucional da UFLA instname:Universidade Federal de Lavras (UFLA) instacron:UFLA |
instname_str |
Universidade Federal de Lavras (UFLA) |
instacron_str |
UFLA |
institution |
UFLA |
reponame_str |
Repositório Institucional da UFLA |
collection |
Repositório Institucional da UFLA |
repository.name.fl_str_mv |
Repositório Institucional da UFLA - Universidade Federal de Lavras (UFLA) |
repository.mail.fl_str_mv |
nivaldo@ufla.br || repositorio.biblioteca@ufla.br |
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1807835230103404544 |