The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3
dc.citation.volume | 12 | |
dc.creator | Steimbrüch, Bruno A. | |
dc.creator | Sartorio, Mariana Gabriela | |
dc.creator | Cortez, Néstor | |
dc.creator | Albanesi, Daniela | |
dc.creator | Lisa, María Natalia | |
dc.creator | Repizo, Guillermo Daniel | |
dc.date.accessioned | 2022-04-05T15:46:59Z | |
dc.date.available | 2022-04-05T15:46:59Z | |
dc.date.issued | 2022-03-12 | |
dc.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. | es |
dc.description.fil | Fil: Steimbrüch, Bruno A. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina. | |
dc.description.fil | Fil: Sartorio, Mariana Gabriela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina. | |
dc.description.fil | Fil: Cortez, Néstor. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina. | |
dc.description.fil | Fil: Albanesi, Daniela. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina. | |
dc.description.fil | Fil: Albanesi, Daniela. Plataforma de Biología Estructural y Metabolómica (PLABEM); Argentina. | |
dc.description.fil | Fil: Lisa, María Natalia. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina. | |
dc.description.fil | Fil: Lisa, María Natalia. Plataforma de Biología Estructural y Metabolómica (PLABEM); Argentina. | |
dc.description.fil | Fil: Repizo, Guillermo Daniel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina. | |
dc.description.sponsorship | Agencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación: PICT 2015–1492 | |
dc.description.sponsorship | Consejo Nacional de Investigaciones Científicas y Técnicas, Argentina (CONICET) | |
dc.format | application/pdf | |
dc.identifier.issn | 2045-2322 | |
dc.identifier.uri | http://hdl.handle.net/2133/23334 | |
dc.language.iso | eng | es |
dc.publisher | Nature Research | es |
dc.relation.publisherversion | https://doi.org/10.1038/s41598-022-08052-z | |
dc.relation.publisherversion | https://www.nature.com/articles/s41598-022-08052-z | |
dc.rights | openAccess | es |
dc.rights.holder | Steimbrüch, Bruno A. | es |
dc.rights.holder | Sartorio, Mariana Gabriela | es |
dc.rights.holder | Cortez, Néstor | es |
dc.rights.holder | Albanesi, Daniela | es |
dc.rights.holder | Lisa, María Natalia | es |
dc.rights.holder | Repizo, Guillermo Daniel | es |
dc.rights.text | Attribution 4.0 International (CC BY 4.0) | es |
dc.subject | Superoxide Dismutase | es |
dc.subject | Gene | es |
dc.subject | Open reading frames | es |
dc.subject | Acinetobacter sp. Ver3 | es |
dc.title | The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3 | es |
dc.type | publishedVersion | |
dc.type | article | |
dc.type | artículo | |
dc.type.collection | articulo | |
dc.type.version | publishedVersion |
Archivos
Bloque original
1 - 1 de 1
Cargando...
- Nombre:
- The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3.pdf
- Tamaño:
- 5.3 MB
- Formato:
- Adobe Portable Document Format
- Descripción:
Bloque de licencias
1 - 1 de 1
- Nombre:
- license.txt
- Tamaño:
- 3.59 KB
- Formato:
- Item-specific license agreed upon to submission
- Descripción: