In silico prediction of protein-protein interaction network induced by manganese II in Meyerozyma guilliermondii.
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | |
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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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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1823329424091643904 |