In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.

Detalhes bibliográficos
Autor(a) principal: Ruas, France Anne Dias
Data de Publicação: 2020
Outros Autores: Cota, Renata Guerra de Sá
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFOP
Texto Completo: http://www.repositorio.ufop.br/jspui/handle/123456789/14014
https://doi.org/10.3389/fmicb.2020.00236
Resumo: Recently, there has been an increasing interest in the use of yeast to produce biosorbent materials, because yeast is economical to use, adaptable to a variety of conditions, and amenable to morphological manipulations to yield better raw biomaterials. Previous studies from our laboratory have shown that Meyerozyma guilliermondii, a nonpathogenic haploid yeast (ascomycete), exhibits excellent biosorption capacity for Mn2+, as demonstrated by kinetic analyses. Shotgun/bottom-up analyses of soluble fractions revealed a total of 1257 identified molecules, with 117 proteins expressed in the absence of Mn2+ and 69 expressed only in the presence of Mn2+. In this article, we describe the first in silico prediction and screening of protein–protein interactions (PPIs) in M. guilliermondii using experimental data from shotgun/bottom-up analyses. We also present the categorization of biological processes (BPs), molecular functions (MFs), and metabolic pathways of 71 proteins upregulated in the M. guilliermondii proteome in response to stress caused by an excess of Mn2+ ions. Most of the annotated proteins were related to oxidation–reduction processes, metabolism, and response to oxidative stress. We identified seven functional enrichments and 42 metabolic pathways; most proteins belonged to pathways related to metabolic pathways (19 proteins) followed by the biosynthesis of secondary metabolites (10 proteins) in the presence of Mn2+. Using our data, it is possible to infer that defense mechanisms minimize the impact of Mn2+ via the expression of antioxidant proteins, thus allowing adjustment during the defense response. Previous studies have not considered protein interactions in this genus in a manner that permits comparisons. Consequently, the findings of the current study are innovative, highly relevant, and provide a description of interactive complexes and networks that yield insight into the cellular processes of M. guilliermondii. Collectively, our data will allow researchers to explore the biotechnological potential of M. guilliermondii in future bioremediation processes.
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spelling In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.BioremediationProteomeMetabolic pathwaysRecently, there has been an increasing interest in the use of yeast to produce biosorbent materials, because yeast is economical to use, adaptable to a variety of conditions, and amenable to morphological manipulations to yield better raw biomaterials. Previous studies from our laboratory have shown that Meyerozyma guilliermondii, a nonpathogenic haploid yeast (ascomycete), exhibits excellent biosorption capacity for Mn2+, as demonstrated by kinetic analyses. Shotgun/bottom-up analyses of soluble fractions revealed a total of 1257 identified molecules, with 117 proteins expressed in the absence of Mn2+ and 69 expressed only in the presence of Mn2+. In this article, we describe the first in silico prediction and screening of protein–protein interactions (PPIs) in M. guilliermondii using experimental data from shotgun/bottom-up analyses. We also present the categorization of biological processes (BPs), molecular functions (MFs), and metabolic pathways of 71 proteins upregulated in the M. guilliermondii proteome in response to stress caused by an excess of Mn2+ ions. Most of the annotated proteins were related to oxidation–reduction processes, metabolism, and response to oxidative stress. We identified seven functional enrichments and 42 metabolic pathways; most proteins belonged to pathways related to metabolic pathways (19 proteins) followed by the biosynthesis of secondary metabolites (10 proteins) in the presence of Mn2+. Using our data, it is possible to infer that defense mechanisms minimize the impact of Mn2+ via the expression of antioxidant proteins, thus allowing adjustment during the defense response. Previous studies have not considered protein interactions in this genus in a manner that permits comparisons. Consequently, the findings of the current study are innovative, highly relevant, and provide a description of interactive complexes and networks that yield insight into the cellular processes of M. guilliermondii. Collectively, our data will allow researchers to explore the biotechnological potential of M. guilliermondii in future bioremediation processes.2021-11-23T15:26:37Z2021-11-23T15:26:37Z2020info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfRUAS, F. A. D.; COTA, R. G. de S. In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii. Frontiers in Microbiology, v. 11, p. 1-14, fev. 2020. Disponível em: <https://www.frontiersin.org/articles/10.3389/fmicb.2020.00236/full>. Acesso em: 10 jun. 2021.1664-302X.http://www.repositorio.ufop.br/jspui/handle/123456789/14014https://doi.org/10.3389/fmicb.2020.00236This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. Source: The article PDF.info:eu-repo/semantics/openAccessRuas, France Anne DiasCota, Renata Guerra de Sáengreponame:Repositório Institucional da UFOPinstname:Universidade Federal de Ouro Preto (UFOP)instacron:UFOP2024-11-10T21:37:59Zoai:repositorio.ufop.br:123456789/14014Repositório InstitucionalPUBhttp://www.repositorio.ufop.br/oai/requestrepositorio@ufop.edu.bropendoar:32332024-11-10T21:37:59Repositório Institucional da UFOP - Universidade Federal de Ouro Preto (UFOP)false
dc.title.none.fl_str_mv In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
title In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
spellingShingle In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
Ruas, France Anne Dias
Bioremediation
Proteome
Metabolic pathways
title_short In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
title_full In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
title_fullStr In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
title_full_unstemmed In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
title_sort In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
author Ruas, France Anne Dias
author_facet Ruas, France Anne Dias
Cota, Renata Guerra de Sá
author_role author
author2 Cota, Renata Guerra de Sá
author2_role author
dc.contributor.author.fl_str_mv Ruas, France Anne Dias
Cota, Renata Guerra de Sá
dc.subject.por.fl_str_mv Bioremediation
Proteome
Metabolic pathways
topic Bioremediation
Proteome
Metabolic pathways
description Recently, there has been an increasing interest in the use of yeast to produce biosorbent materials, because yeast is economical to use, adaptable to a variety of conditions, and amenable to morphological manipulations to yield better raw biomaterials. Previous studies from our laboratory have shown that Meyerozyma guilliermondii, a nonpathogenic haploid yeast (ascomycete), exhibits excellent biosorption capacity for Mn2+, as demonstrated by kinetic analyses. Shotgun/bottom-up analyses of soluble fractions revealed a total of 1257 identified molecules, with 117 proteins expressed in the absence of Mn2+ and 69 expressed only in the presence of Mn2+. In this article, we describe the first in silico prediction and screening of protein–protein interactions (PPIs) in M. guilliermondii using experimental data from shotgun/bottom-up analyses. We also present the categorization of biological processes (BPs), molecular functions (MFs), and metabolic pathways of 71 proteins upregulated in the M. guilliermondii proteome in response to stress caused by an excess of Mn2+ ions. Most of the annotated proteins were related to oxidation–reduction processes, metabolism, and response to oxidative stress. We identified seven functional enrichments and 42 metabolic pathways; most proteins belonged to pathways related to metabolic pathways (19 proteins) followed by the biosynthesis of secondary metabolites (10 proteins) in the presence of Mn2+. Using our data, it is possible to infer that defense mechanisms minimize the impact of Mn2+ via the expression of antioxidant proteins, thus allowing adjustment during the defense response. Previous studies have not considered protein interactions in this genus in a manner that permits comparisons. Consequently, the findings of the current study are innovative, highly relevant, and provide a description of interactive complexes and networks that yield insight into the cellular processes of M. guilliermondii. Collectively, our data will allow researchers to explore the biotechnological potential of M. guilliermondii in future bioremediation processes.
publishDate 2020
dc.date.none.fl_str_mv 2020
2021-11-23T15:26:37Z
2021-11-23T15:26:37Z
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 RUAS, F. A. D.; COTA, R. G. de S. In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii. Frontiers in Microbiology, v. 11, p. 1-14, fev. 2020. Disponível em: <https://www.frontiersin.org/articles/10.3389/fmicb.2020.00236/full>. Acesso em: 10 jun. 2021.
1664-302X.
http://www.repositorio.ufop.br/jspui/handle/123456789/14014
https://doi.org/10.3389/fmicb.2020.00236
identifier_str_mv RUAS, F. A. D.; COTA, R. G. de S. In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii. Frontiers in Microbiology, v. 11, p. 1-14, fev. 2020. Disponível em: <https://www.frontiersin.org/articles/10.3389/fmicb.2020.00236/full>. Acesso em: 10 jun. 2021.
1664-302X.
url http://www.repositorio.ufop.br/jspui/handle/123456789/14014
https://doi.org/10.3389/fmicb.2020.00236
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Institucional da UFOP
instname:Universidade Federal de Ouro Preto (UFOP)
instacron:UFOP
instname_str Universidade Federal de Ouro Preto (UFOP)
instacron_str UFOP
institution UFOP
reponame_str Repositório Institucional da UFOP
collection Repositório Institucional da UFOP
repository.name.fl_str_mv Repositório Institucional da UFOP - Universidade Federal de Ouro Preto (UFOP)
repository.mail.fl_str_mv repositorio@ufop.edu.br
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