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A strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by Betaproteobacteria species
Nonribosomal peptides have an important pharmacological role due to their extensive biological properties. The singularities in the biosynthesis of these natural products allowed the development of genome-mining strategies which associate them to their original biosynthetic gene clusters. Generally,...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5583390/ https://www.ncbi.nlm.nih.gov/pubmed/28871139 http://dx.doi.org/10.1038/s41598-017-11314-w |
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author | Baldim, João Luiz da Silva, Bruna Lidiane Chagas-Paula, Daniela Aparecida Lago, João Henrique G. Soares, Marisi G. |
author_facet | Baldim, João Luiz da Silva, Bruna Lidiane Chagas-Paula, Daniela Aparecida Lago, João Henrique G. Soares, Marisi G. |
author_sort | Baldim, João Luiz |
collection | PubMed |
description | Nonribosomal peptides have an important pharmacological role due to their extensive biological properties. The singularities in the biosynthesis of these natural products allowed the development of genome-mining strategies which associate them to their original biosynthetic gene clusters. Generally, these compounds present complex architectures that make their identification difficult. Based on these evidences, genomes from species of the class Betaproteobacteria were studied with the purpose of finding biosynthetic similarities among them. These organisms were applied as templates due to their large number of biosynthetic gene clusters and the natural products isolated from them. The strategy for Rapid Identification of Nonribosomal Peptides Portions (RINPEP) proposed in this work was built by reorganizing the data obtained from antiSMASH and NCBI with a product-centered way. The verification steps of RINPEP comprehended the fragments of existent compounds and predictions obtained in silico with the purpose of finding common subunits expressed by different genomic sequences. The results of this strategy revealed patterns in a global overview of the biosynthesis of nonribosomal peptides by Betaproteobacteria. |
format | Online Article Text |
id | pubmed-5583390 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-55833902017-09-06 A strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by Betaproteobacteria species Baldim, João Luiz da Silva, Bruna Lidiane Chagas-Paula, Daniela Aparecida Lago, João Henrique G. Soares, Marisi G. Sci Rep Article Nonribosomal peptides have an important pharmacological role due to their extensive biological properties. The singularities in the biosynthesis of these natural products allowed the development of genome-mining strategies which associate them to their original biosynthetic gene clusters. Generally, these compounds present complex architectures that make their identification difficult. Based on these evidences, genomes from species of the class Betaproteobacteria were studied with the purpose of finding biosynthetic similarities among them. These organisms were applied as templates due to their large number of biosynthetic gene clusters and the natural products isolated from them. The strategy for Rapid Identification of Nonribosomal Peptides Portions (RINPEP) proposed in this work was built by reorganizing the data obtained from antiSMASH and NCBI with a product-centered way. The verification steps of RINPEP comprehended the fragments of existent compounds and predictions obtained in silico with the purpose of finding common subunits expressed by different genomic sequences. The results of this strategy revealed patterns in a global overview of the biosynthesis of nonribosomal peptides by Betaproteobacteria. Nature Publishing Group UK 2017-09-04 /pmc/articles/PMC5583390/ /pubmed/28871139 http://dx.doi.org/10.1038/s41598-017-11314-w Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Baldim, João Luiz da Silva, Bruna Lidiane Chagas-Paula, Daniela Aparecida Lago, João Henrique G. Soares, Marisi G. A strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by Betaproteobacteria species |
title | A strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by Betaproteobacteria species |
title_full | A strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by Betaproteobacteria species |
title_fullStr | A strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by Betaproteobacteria species |
title_full_unstemmed | A strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by Betaproteobacteria species |
title_short | A strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by Betaproteobacteria species |
title_sort | strategy for the identification of patterns in the biosynthesis of nonribosomal peptides by betaproteobacteria species |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5583390/ https://www.ncbi.nlm.nih.gov/pubmed/28871139 http://dx.doi.org/10.1038/s41598-017-11314-w |
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