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 principales: Steimbrüch, Bruno A., Sartorio, Mariana Gabriela, Cortez, Néstor, Albanesi, Daniela, Lisa, María Natalia, Repizo, Guillermo Daniel
Lenguaje:Inglés
Publicado: Nature Research 2022
Materias:
Superoxide Dismutase
Gene
Open reading frames
Acinetobacter sp. Ver3
Acceso en línea:http://hdl.handle.net/2133/23334
http://hdl.handle.net/2133/23334
Aporte de:
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) de Universidad Nacional de Rosario
id I15-R121-2133-23334
record_format dspace
institution Universidad Nacional de Rosario
institution_str I-15
repository_str R-121
collection Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR)
language Inglés
orig_language_str_mv eng
topic Superoxide Dismutase
Gene
Open reading frames
Acinetobacter sp. Ver3
spellingShingle Superoxide Dismutase
Gene
Open reading frames
Acinetobacter sp. Ver3
Steimbrüch, Bruno A.
Sartorio, Mariana Gabriela
Cortez, Néstor
Albanesi, Daniela
Lisa, María Natalia
Repizo, Guillermo Daniel
The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
topic_facet Superoxide Dismutase
Gene
Open reading frames
Acinetobacter sp. Ver3
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 Acinetobacter spp. are confronted with oxidizing agents.
author Steimbrüch, Bruno A.
Sartorio, Mariana Gabriela
Cortez, Néstor
Albanesi, Daniela
Lisa, María Natalia
Repizo, Guillermo Daniel
author_facet Steimbrüch, Bruno A.
Sartorio, Mariana Gabriela
Cortez, Néstor
Albanesi, Daniela
Lisa, María Natalia
Repizo, Guillermo Daniel
author_sort Steimbrüch, Bruno A.
title The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
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 distinctive roles played by the superoxide dismutases of the extremophile acinetobacter sp. ver3
publisher Nature Research
publishDate 2022
url http://hdl.handle.net/2133/23334
http://hdl.handle.net/2133/23334
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