Catalases of the polyextremophylic andean isolate Acinetobacter sp. Ver 3 confer adaptive response to H2O2 and UV radiation

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dc.citation.titleThe FEBS Journal
dc.citation.volume287
dc.contributor.orcidhttps://orcid.org/0000-0003-1318-8738
dc.contributor.otherPerdomo, Virginia: assistance with qRT-PCR measurements
dc.contributor.otherDr. Carrillo, Néstor: review of the manuscript
dc.creatorSartorio, Mariana Gabriela
dc.creatorRepizo, Guillermo Daniel
dc.creatorCortez, Néstor
dc.date.accessioned2024-06-03T19:56:41Z
dc.date.available2024-06-03T19:56:41Z
dc.date.issued2020-02-09
dc.description.abstractThe polyextremophilic strain Acinetobacter sp. Ver3 isolated from high-altitude Andean lakes exhibits elevated tolerance to UV-B radiation and to pro-oxidants, a feature that has been correlated to its unusually high catalase activity. The Ver3 genome sequence analysis revealed the presence of two genes coding for monofunctional catalases: AV3KatE1 and AV3KatE2, the latter harboring an N-terminal signal peptide. We show herein that AV3KatE1 displays one of the highest catalytic activities reported so far and is constitutively expressed at relatively high amounts in the cytosol, acting as the main protecting catalase against H2O2 and UV-B radiation. The second catalase, AV3KatE2, is a periplasmic enzyme strongly induced by both peroxide and UV, conferring supplementary protection against pro-oxidants. The N-terminal signal present in AV3KatE2 was required not only for transport to the periplasm via the twin-arginine translocation pathway, but also for proper folding and subsequent catalytic activity. The analysis of catalase distribution among 114 Acinetobacter complete genomes revealed a great variability in the catalase classes, with A. baumannii clinical isolates exhibiting higher numbers of isoenzymes and the most variable profiles.
dc.description.filFil: Sartorio, Mariana Gabriela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Repizo, Guillermo Daniel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Cortez, Néstor. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.sponsorshipAgencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación (Agencia I+D+i): PICT 2015-1492
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Técnicas (CONICET)
dc.description.versionpeerreviewed
dc.format.extent1-15
dc.identifier.e-issn1742-4658
dc.identifier.issn1742-464X
dc.identifier.urihttps://hdl.handle.net/2133/27147
dc.language.isoen
dc.publisherWiley
dc.relation.publisherversionhttps://doi.org/10.1111/febs.15244
dc.relation.publisherversionhttps://febs.onlinelibrary.wiley.com/doi/10.1111/febs.15244
dc.rightsopenAccess
dc.rights.holderSartorio, Mariana Gabriela
dc.rights.holderRepizo, Guillermo Daniel
dc.rights.holderCortez, Néstor
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas
dc.rights.textAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectAcinetobacter
dc.subjectAndean wetlands
dc.subjectCatalase
dc.subjectOxidative stress
dc.subjectUV radiation
dc.titleCatalases of the polyextremophylic andean isolate Acinetobacter sp. Ver 3 confer adaptive response to H2O2 and UV radiation
dc.typearticulo
dc.type.versionpublishedVersion

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