The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3

Acinetobacter sp. Ver3 is a polyextremophilic strain characterized by a high tolerance to radiation and pro-oxidants. The Ver3 genome comprises the sodB and sodC genes encoding an iron (AV3SodB) and a copper/zinc superoxide dismutase (AV3SodC), respectively; however, the specific role(s) of these ge...

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Detalles Bibliográficos
Autores: Steimbrüch, Bruno Alejandro, Sartorio, Mariana Gabriela, Cortez, Nestor Ricardo, Albanesi, Daniela, Lisa, María Natalia, Repizo, Guillermo Daniel
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/213377
Acceso en línea:http://hdl.handle.net/11336/213377
Access Level:acceso abierto
Palabra clave:ANDEAN LAKES
ACINETOBACTER
UV RADIATION
OXIDATIVE STRESS
SUPEROXIDE DISMUTASE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
id AR_c2726cd4e4600a70f034383da4194247
oai_identifier_str oai:ri.conicet.gov.ar:11336/213377
network_acronym_str AR
network_name_str Argentina
repository_id_str
dc.title.none.fl_str_mv The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
title The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
spellingShingle The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
Steimbrüch, Bruno Alejandro
ANDEAN LAKES
ACINETOBACTER
UV RADIATION
OXIDATIVE STRESS
SUPEROXIDE DISMUTASE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
title_full The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
title_fullStr The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
title_full_unstemmed The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
title_sort The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
dc.creator.none.fl_str_mv Steimbrüch, Bruno Alejandro
Sartorio, Mariana Gabriela
Cortez, Nestor Ricardo
Albanesi, Daniela
Lisa, María Natalia
Repizo, Guillermo Daniel
author Steimbrüch, Bruno Alejandro
author_facet Steimbrüch, Bruno Alejandro
Sartorio, Mariana Gabriela
Cortez, Nestor Ricardo
Albanesi, Daniela
Lisa, María Natalia
Repizo, Guillermo Daniel
author_role author
author2 Sartorio, Mariana Gabriela
Cortez, Nestor Ricardo
Albanesi, Daniela
Lisa, María Natalia
Repizo, Guillermo Daniel
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv ANDEAN LAKES
ACINETOBACTER
UV RADIATION
OXIDATIVE STRESS
SUPEROXIDE DISMUTASE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic ANDEAN LAKES
ACINETOBACTER
UV RADIATION
OXIDATIVE STRESS
SUPEROXIDE DISMUTASE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description Acinetobacter sp. Ver3 is a polyextremophilic strain characterized by a high tolerance to radiation and pro-oxidants. The Ver3 genome comprises the sodB and sodC genes encoding an iron (AV3SodB) and a copper/zinc superoxide dismutase (AV3SodC), respectively; however, the specific role(s) of these genes has remained elusive. We show that the expression of sodB remained unaltered in different oxidative stress conditions whereas sodC was up-regulated in the presence of blue light. Besides, we studied the changes in the in vitro activity of each SOD enzyme in response to diverse agents and solved the crystal structure of AV3SodB at 1.34 Å, one of the highest resolutions achieved for a SOD. Cell fractionation studies interestingly revealed that AV3SodB is located in the cytosol whereas AV3SodC is also found in the periplasm. Consistently, a bioinformatic analysis of the genomes of 53 Acinetobacter species pointed out the presence of at least one SOD type in each compartment, suggesting that these enzymes are separately required to cope with oxidative stress. Surprisingly, AV3SodC was found in an active state also in outer membrane vesicles, probably exerting a protective role. Overall, our multidisciplinary approach highlights the relevance of SOD enzymes when Acinetobacterspp. are confronted with oxidizing agents.
publishDate 2022
dc.date.none.fl_str_mv 2022-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/213377
Steimbrüch, Bruno Alejandro; Sartorio, Mariana Gabriela; Cortez, Nestor Ricardo; Albanesi, Daniela; Lisa, María Natalia; et al.; The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3; Nature Publishing Group; Scientific Reports; 12; 1; 3-2022; 1-15
2045-2322
CONICET Digital
CONICET
url http://hdl.handle.net/11336/213377
identifier_str_mv Steimbrüch, Bruno Alejandro; Sartorio, Mariana Gabriela; Cortez, Nestor Ricardo; Albanesi, Daniela; Lisa, María Natalia; et al.; The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3; Nature Publishing Group; Scientific Reports; 12; 1; 3-2022; 1-15
2045-2322
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-022-08052-z
info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-022-08052-z
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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spelling The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3Steimbrüch, Bruno AlejandroSartorio, Mariana GabrielaCortez, Nestor RicardoAlbanesi, DanielaLisa, María NataliaRepizo, Guillermo DanielANDEAN LAKESACINETOBACTERUV RADIATIONOXIDATIVE STRESSSUPEROXIDE DISMUTASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Acinetobacter sp. Ver3 is a polyextremophilic strain characterized by a high tolerance to radiation and pro-oxidants. The Ver3 genome comprises the sodB and sodC genes encoding an iron (AV3SodB) and a copper/zinc superoxide dismutase (AV3SodC), respectively; however, the specific role(s) of these genes has remained elusive. We show that the expression of sodB remained unaltered in different oxidative stress conditions whereas sodC was up-regulated in the presence of blue light. Besides, we studied the changes in the in vitro activity of each SOD enzyme in response to diverse agents and solved the crystal structure of AV3SodB at 1.34 Å, one of the highest resolutions achieved for a SOD. Cell fractionation studies interestingly revealed that AV3SodB is located in the cytosol whereas AV3SodC is also found in the periplasm. Consistently, a bioinformatic analysis of the genomes of 53 Acinetobacter species pointed out the presence of at least one SOD type in each compartment, suggesting that these enzymes are separately required to cope with oxidative stress. Surprisingly, AV3SodC was found in an active state also in outer membrane vesicles, probably exerting a protective role. Overall, our multidisciplinary approach highlights the relevance of SOD enzymes when Acinetobacterspp. are confronted with oxidizing agents.Fil: Steimbrüch, Bruno Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Sartorio, Mariana Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Cortez, Nestor Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Albanesi, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Lisa, María Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Repizo, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaNature Publishing Group2022-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/213377Steimbrüch, Bruno Alejandro; Sartorio, Mariana Gabriela; Cortez, Nestor Ricardo; Albanesi, Daniela; Lisa, María Natalia; et al.; The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3; Nature Publishing Group; Scientific Reports; 12; 1; 3-2022; 1-152045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-022-08052-zinfo:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-022-08052-zinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T14:27:42Zoai:ri.conicet.gov.ar:11336/213377instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982024-05-08 14:27:43.241CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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