A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Research, Society and Development |
Texto Completo: | https://rsdjournal.org/index.php/rsd/article/view/12714 |
Resumo: | Anhydrobiosis refers to a state of suspended animation in which some organisms enter when exposed to extreme desiccation, ensuring them an outstanding tolerance to several physical stresses due to molecular and cellular adaptations. Metallothioneins (MTs) are short cysteine-rich metal-chelating proteins that work as a cellular protection element in metal ion-rich conditions. Here we aimed to investigate possible molecular signatures in primary and tertiary structures in anhydrobiotic cyanobacterial MTs. Anhydrobiotic and non-anhydrobiotic cyanobacterial MT amino acid sequences were retrieved from NCBI database and aligned in Clustal Omega server. Additionally, the amino acid compositions of these sequences were determined by GeneRunner. Further, we carried out homology-modeling via SWISS-MODEL, structural superposition in UCSF Chimera 1.4 Matchmaker tool and ligand-binding site prediction via COFACTOR. In silico analyses revealed specific divergences in amino acid positions between MT groups, evidencing positive and negative selections, however without affecting final protein structures. Some of these changes on polypeptide sequence potentially enhance protein stabilization during desiccation, whereas others possibly act as additional metal-ion coordinating residues. Analyses on the molecular adaptations on anhydrobiotic cyanobacterial MTs help shed light on their molecular functions and biological roles, as well as may have applications on the development of desiccation- and metal-tolerant organisms. |
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A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneinsUna firma molecular distinta en las metalotioneínas de cianobactérias anhidrobióticasUma assinatura molecular distinta em metalotioneínas de cianobactérias anidrobióticasAnidrobioseCOFACTORCianobactériaModelagem por homologiaMetalotioneínaSWISS-MODEL.AnhidrobiosisCOFACTORCianobacteriaModelado de homologiaMetalotioneínaSWISS-MODEL.AnhydrobiosisCOFACTORCyanobacteriaHomology-modelingMetallothioneinSWISS-MODEL.Anhydrobiosis refers to a state of suspended animation in which some organisms enter when exposed to extreme desiccation, ensuring them an outstanding tolerance to several physical stresses due to molecular and cellular adaptations. Metallothioneins (MTs) are short cysteine-rich metal-chelating proteins that work as a cellular protection element in metal ion-rich conditions. Here we aimed to investigate possible molecular signatures in primary and tertiary structures in anhydrobiotic cyanobacterial MTs. Anhydrobiotic and non-anhydrobiotic cyanobacterial MT amino acid sequences were retrieved from NCBI database and aligned in Clustal Omega server. Additionally, the amino acid compositions of these sequences were determined by GeneRunner. Further, we carried out homology-modeling via SWISS-MODEL, structural superposition in UCSF Chimera 1.4 Matchmaker tool and ligand-binding site prediction via COFACTOR. In silico analyses revealed specific divergences in amino acid positions between MT groups, evidencing positive and negative selections, however without affecting final protein structures. Some of these changes on polypeptide sequence potentially enhance protein stabilization during desiccation, whereas others possibly act as additional metal-ion coordinating residues. Analyses on the molecular adaptations on anhydrobiotic cyanobacterial MTs help shed light on their molecular functions and biological roles, as well as may have applications on the development of desiccation- and metal-tolerant organisms.La anhidrobiosis se refiere a un estado de animación suspendida en el que entran algunos organismos cuando están expuestos a una desecación extrema, lo que les garantiza una tolerancia a diversos estresantes físicos debido a adaptaciones moleculares y celulares. Las metalotioneínas (MTs) son pequeñas proteínas quelantes de metales ricas en cisteínas que actúan como un elemento de protección a las células en condiciones ricas en iones metálicos. Aquí, nuestro objetivo fue investigar posibles firmas moleculares en estructuras primarias y terciarias de MT en cianobacterias anhidrobióticas. Se recuperaron las secuencias de aminoácidos de MTs de cianobacterias anhidrobióticas y no anhidrobióticas de la base de datos NCBI y se las alineó en el servidor Clustal Omega. Además, se determinaron las composiciones de aminoácidos de estas secuencias con el software GeneRunner. Posteriormente, realizamos el modelado por homología vía SWISS-MODEL, la superposición estructural con la herramienta UCSF Chimera 1.4 Matchmaker y la predicción del sitio de unión por el COFACTOR. Los análisis in silico revelaron divergencias específicas entre los grupos de MTs, evidenciando selecciones positivas y negativas, con todo, sin afectar la estructura final de estas proteínas. Algunos de estos cambios en la secuencia polipeptídica pueden mejorar la estabilización proteica durante la desecación, mientras que otros posiblemente actúan como residuos de coordinación de iones metálicos. Los análisis de las adaptaciones moleculares de metalotioneínas de cianobacterias anhidrobióticas pueden elucidar sus funciones moleculares y en sus papeles biológicos, así como pueden presentar aplicaciones en el desarrollo de organismos tolerantes a la desecación y a los metales.Anidrobiose refere-se a um estado de animação suspensa no qual alguns organismos entram quando são expostos à dessecação extrema, garantindo a eles uma tolerância a diversos estresses físicos, devido a adaptações moleculares e celulares. Metalotioneínas (MTs) são pequenas proteínas quelantes de metais e ricas em cisteínas que atuam como um elemento de proteção às células em condições ricas em íons metálicos. Aqui, nós buscamos investigar possíveis assinaturas moleculares em estruturas primárias e terciárias de MTs de cianobactérias anidrobióticas. Sequências de aminoácidos de MTs de cianobactérias anidrobióticas e não-anidrobióticas foram obtidas no banco de dados NCBI e alinhadas no servidor Clustal Omega. Adicionalmente, as composições de aminoácidos destas sequências foram determinadas pelo software GeneRunner. Em seguida, nós realizamos modelagem por homologia via SWISS-MODEL, sobreposição estrutural pela ferramenta UCSF Chimera 1.4 Matchmaker e a predição de sítios de ligação via COFACTOR. As análises in silico revelaram divergências específicas nas posições de aminoácidos entre os grupos de MTs, evidenciando seleções positivas e negativas, porém, sem afetar a estrutura final destas proteínas. Algumas destas mudanças na sequência polipeptídica têm potencial em aumentar a estabilização proteica durante a dessecação, enquanto outras podem atuar como resíduos coordenantes de íons metálicos. Análises das adaptações moleculares de metalotioneínas de cianobactérias anidrobióticas podem ajudar a jogar luz em suas funções moleculares e em seus papéis biológicos, assim como podem apresentar aplicações no desenvolvimento de organismos tolerantes à dessecação e a metais.Research, Society and Development2021-02-27info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://rsdjournal.org/index.php/rsd/article/view/1271410.33448/rsd-v10i2.12714Research, Society and Development; Vol. 10 No. 2; e50610212714Research, Society and Development; Vol. 10 Núm. 2; e50610212714Research, Society and Development; v. 10 n. 2; e506102127142525-3409reponame:Research, Society and Developmentinstname:Universidade Federal de Itajubá (UNIFEI)instacron:UNIFEIenghttps://rsdjournal.org/index.php/rsd/article/view/12714/11547Copyright (c) 2021 Danyel Fernandes Contiliani; Vitor Nolasco de Moraes; Yasmin de Araújo Ribeiro; Tiago Campos Pereirahttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessContiliani, Danyel Fernandes Moraes, Vitor Nolasco de Ribeiro, Yasmin de Araújo Pereira, Tiago Campos 2021-03-02T09:32:39Zoai:ojs.pkp.sfu.ca:article/12714Revistahttps://rsdjournal.org/index.php/rsd/indexPUBhttps://rsdjournal.org/index.php/rsd/oairsd.articles@gmail.com2525-34092525-3409opendoar:2024-01-17T09:34:13.121455Research, Society and Development - Universidade Federal de Itajubá (UNIFEI)false |
dc.title.none.fl_str_mv |
A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins Una firma molecular distinta en las metalotioneínas de cianobactérias anhidrobióticas Uma assinatura molecular distinta em metalotioneínas de cianobactérias anidrobióticas |
title |
A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins |
spellingShingle |
A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins Contiliani, Danyel Fernandes Anidrobiose COFACTOR Cianobactéria Modelagem por homologia Metalotioneína SWISS-MODEL. Anhidrobiosis COFACTOR Cianobacteria Modelado de homologia Metalotioneína SWISS-MODEL. Anhydrobiosis COFACTOR Cyanobacteria Homology-modeling Metallothionein SWISS-MODEL. |
title_short |
A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins |
title_full |
A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins |
title_fullStr |
A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins |
title_full_unstemmed |
A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins |
title_sort |
A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins |
author |
Contiliani, Danyel Fernandes |
author_facet |
Contiliani, Danyel Fernandes Moraes, Vitor Nolasco de Ribeiro, Yasmin de Araújo Pereira, Tiago Campos |
author_role |
author |
author2 |
Moraes, Vitor Nolasco de Ribeiro, Yasmin de Araújo Pereira, Tiago Campos |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Contiliani, Danyel Fernandes Moraes, Vitor Nolasco de Ribeiro, Yasmin de Araújo Pereira, Tiago Campos |
dc.subject.por.fl_str_mv |
Anidrobiose COFACTOR Cianobactéria Modelagem por homologia Metalotioneína SWISS-MODEL. Anhidrobiosis COFACTOR Cianobacteria Modelado de homologia Metalotioneína SWISS-MODEL. Anhydrobiosis COFACTOR Cyanobacteria Homology-modeling Metallothionein SWISS-MODEL. |
topic |
Anidrobiose COFACTOR Cianobactéria Modelagem por homologia Metalotioneína SWISS-MODEL. Anhidrobiosis COFACTOR Cianobacteria Modelado de homologia Metalotioneína SWISS-MODEL. Anhydrobiosis COFACTOR Cyanobacteria Homology-modeling Metallothionein SWISS-MODEL. |
description |
Anhydrobiosis refers to a state of suspended animation in which some organisms enter when exposed to extreme desiccation, ensuring them an outstanding tolerance to several physical stresses due to molecular and cellular adaptations. Metallothioneins (MTs) are short cysteine-rich metal-chelating proteins that work as a cellular protection element in metal ion-rich conditions. Here we aimed to investigate possible molecular signatures in primary and tertiary structures in anhydrobiotic cyanobacterial MTs. Anhydrobiotic and non-anhydrobiotic cyanobacterial MT amino acid sequences were retrieved from NCBI database and aligned in Clustal Omega server. Additionally, the amino acid compositions of these sequences were determined by GeneRunner. Further, we carried out homology-modeling via SWISS-MODEL, structural superposition in UCSF Chimera 1.4 Matchmaker tool and ligand-binding site prediction via COFACTOR. In silico analyses revealed specific divergences in amino acid positions between MT groups, evidencing positive and negative selections, however without affecting final protein structures. Some of these changes on polypeptide sequence potentially enhance protein stabilization during desiccation, whereas others possibly act as additional metal-ion coordinating residues. Analyses on the molecular adaptations on anhydrobiotic cyanobacterial MTs help shed light on their molecular functions and biological roles, as well as may have applications on the development of desiccation- and metal-tolerant organisms. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-02-27 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://rsdjournal.org/index.php/rsd/article/view/12714 10.33448/rsd-v10i2.12714 |
url |
https://rsdjournal.org/index.php/rsd/article/view/12714 |
identifier_str_mv |
10.33448/rsd-v10i2.12714 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
https://rsdjournal.org/index.php/rsd/article/view/12714/11547 |
dc.rights.driver.fl_str_mv |
https://creativecommons.org/licenses/by/4.0 info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/4.0 |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Research, Society and Development |
publisher.none.fl_str_mv |
Research, Society and Development |
dc.source.none.fl_str_mv |
Research, Society and Development; Vol. 10 No. 2; e50610212714 Research, Society and Development; Vol. 10 Núm. 2; e50610212714 Research, Society and Development; v. 10 n. 2; e50610212714 2525-3409 reponame:Research, Society and Development instname:Universidade Federal de Itajubá (UNIFEI) instacron:UNIFEI |
instname_str |
Universidade Federal de Itajubá (UNIFEI) |
instacron_str |
UNIFEI |
institution |
UNIFEI |
reponame_str |
Research, Society and Development |
collection |
Research, Society and Development |
repository.name.fl_str_mv |
Research, Society and Development - Universidade Federal de Itajubá (UNIFEI) |
repository.mail.fl_str_mv |
rsd.articles@gmail.com |
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1797052745747791872 |