The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
Abstract 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...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2022-03-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-022-08052-z |
| _version_ | 1819294544993189888 |
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| author | Bruno Alejandro Steimbrüch Mariana Gabriela Sartorio Néstor Cortez Daniela Albanesi María-Natalia Lisa Guillermo Daniel Repizo |
| author_facet | Bruno Alejandro Steimbrüch Mariana Gabriela Sartorio Néstor Cortez Daniela Albanesi María-Natalia Lisa Guillermo Daniel Repizo |
| author_sort | Bruno Alejandro Steimbrüch |
| collection | DOAJ |
| description | Abstract 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. |
| first_indexed | 2024-12-24T04:28:01Z |
| format | Article |
| id | doaj.art-95ebb0ef3f7d46598948b6e80185920a |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-24T04:28:01Z |
| publishDate | 2022-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-95ebb0ef3f7d46598948b6e80185920a2022-12-21T17:15:30ZengNature PortfolioScientific Reports2045-23222022-03-0112111510.1038/s41598-022-08052-zThe distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3Bruno Alejandro Steimbrüch0Mariana Gabriela Sartorio1Néstor Cortez2Daniela Albanesi3María-Natalia Lisa4Guillermo Daniel Repizo5Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET), Departamento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de RosarioInstituto de Biología Molecular y Celular de Rosario (IBR, CONICET), Departamento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de RosarioInstituto de Biología Molecular y Celular de Rosario (IBR, CONICET), Departamento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de RosarioInstituto de Biología Molecular y Celular de Rosario (IBR, CONICET-UNR)Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET-UNR)Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET), Departamento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de RosarioAbstract 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.https://doi.org/10.1038/s41598-022-08052-z |
| spellingShingle | Bruno Alejandro Steimbrüch Mariana Gabriela Sartorio Néstor Cortez Daniela Albanesi María-Natalia Lisa Guillermo Daniel Repizo The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3 Scientific Reports |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41598-022-08052-z |
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