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The distinctive roles played by the superoxide dismutases of the extremophile Acinetobactersp. 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 ((AV3)SodB) and a copper/zinc superoxide dismutase ((AV3)SodC), respectively; however, the specific role(s) of thes...

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Autores principales: Steimbrüch, Bruno Alejandro, Sartorio, Mariana Gabriela, Cortez, Néstor, Albanesi, Daniela, Lisa, María-Natalia, Repizo, Guillermo Daniel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8918354/
https://www.ncbi.nlm.nih.gov/pubmed/35279679
http://dx.doi.org/10.1038/s41598-022-08052-z
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author Steimbrüch, Bruno Alejandro
Sartorio, Mariana Gabriela
Cortez, Néstor
Albanesi, Daniela
Lisa, María-Natalia
Repizo, Guillermo Daniel
author_facet Steimbrüch, Bruno Alejandro
Sartorio, Mariana Gabriela
Cortez, Néstor
Albanesi, Daniela
Lisa, María-Natalia
Repizo, Guillermo Daniel
author_sort Steimbrüch, Bruno Alejandro
collection PubMed
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 ((AV3)SodB) and a copper/zinc superoxide dismutase ((AV3)SodC), 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 (AV3)SodB at 1.34 Å, one of the highest resolutions achieved for a SOD. Cell fractionation studies interestingly revealed that (AV3)SodB is located in the cytosol whereas (AV3)SodC 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, (AV3)SodC 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 Acinetobacter spp. are confronted with oxidizing agents.
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spelling pubmed-89183542022-03-16 The distinctive roles played by the superoxide dismutases of the extremophile Acinetobactersp. Ver3 Steimbrüch, Bruno Alejandro Sartorio, Mariana Gabriela Cortez, Néstor Albanesi, Daniela Lisa, María-Natalia Repizo, Guillermo Daniel Sci Rep Article 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 ((AV3)SodB) and a copper/zinc superoxide dismutase ((AV3)SodC), 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 (AV3)SodB at 1.34 Å, one of the highest resolutions achieved for a SOD. Cell fractionation studies interestingly revealed that (AV3)SodB is located in the cytosol whereas (AV3)SodC 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, (AV3)SodC 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 Acinetobacter spp. are confronted with oxidizing agents. Nature Publishing Group UK 2022-03-12 /pmc/articles/PMC8918354/ /pubmed/35279679 http://dx.doi.org/10.1038/s41598-022-08052-z Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Steimbrüch, Bruno Alejandro
Sartorio, Mariana Gabriela
Cortez, Néstor
Albanesi, Daniela
Lisa, María-Natalia
Repizo, Guillermo Daniel
The distinctive roles played by the superoxide dismutases of the extremophile Acinetobactersp. Ver3
title The distinctive roles played by the superoxide dismutases of the extremophile Acinetobactersp. Ver3
title_full The distinctive roles played by the superoxide dismutases of the extremophile Acinetobactersp. Ver3
title_fullStr The distinctive roles played by the superoxide dismutases of the extremophile Acinetobactersp. Ver3
title_full_unstemmed The distinctive roles played by the superoxide dismutases of the extremophile Acinetobactersp. Ver3
title_short The distinctive roles played by the superoxide dismutases of the extremophile Acinetobactersp. Ver3
title_sort distinctive roles played by the superoxide dismutases of the extremophile acinetobactersp. ver3
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8918354/
https://www.ncbi.nlm.nih.gov/pubmed/35279679
http://dx.doi.org/10.1038/s41598-022-08052-z
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