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Título: | Plant catalases as NO and H2S targets |
Autor: | Palma Martínez, José Manuel CSIC ORCID; Mateos Bernal, Rosa María CSIC ORCID; López-Jaramillo, Javier CSIC ORCID; Rodríguez-Ruiz, Marta CSIC ORCID; González-Gordo, Salvador CSIC ORCID; Lechuga-Sancho, Alfonso María; Corpas, Francisco J. CSIC ORCID | Palabras clave: | Docking Nitration S-nitrosation Persulfidation Post-translational modifications Signaling |
Fecha de publicación: | 2020 | Editor: | Elsevier | Citación: | Redox Biology 34: 101525 (2020) | Resumen: | Catalase is a powerful antioxidant metalloenzyme located in peroxisomes which also plays a central role in signaling processes under physiological and adverse situations. Whereas animals contain a single catalase gene, in plants this enzyme is encoded by a multigene family providing multiple isoenzymes whose number varies depending on the species, and their expression is regulated according to their tissue/organ distribution and the environmental conditions. This enzyme can be modulated by reactive oxygen and nitrogen species (ROS/RNS) as well as by hydrogen sulfide (HS). Catalase is the major protein undergoing Tyr-nitration [post-translational modification (PTM) promoted by RNS] during fruit ripening, but the enzyme from diverse sources is also susceptible to undergo other activity-modifying PTMs. Data on S-nitrosation and persulfidation of catalase from different plant origins are given and compared here with results from obese children where S-nitrosation of catalase occurs. The cysteine residues prone to be S-nitrosated in catalase from plants and from bovine liver have been identified. These evidences assign to peroxisomes a crucial statement in the signaling crossroads among relevant molecules (NO and HS), since catalase is allocated in these organelles. This review depicts a scenario where the regulation of catalase through PTMs, especially S-nitrosation and persulfidation, is highlighted. | Versión del editor: | http://dx.doi.org/10.1016/j.redox.2020.101525 | URI: | http://hdl.handle.net/10261/218290 | DOI: | 10.1016/j.redox.2020.101525 | Identificadores: | doi: 10.1016/j.redox.2020.101525 issn: 2213-2317 |
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2020_Palma_RB_OA.pdf | 1,19 MB | Adobe PDF | Visualizar/Abrir |
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