Regulating the regulator: nitric oxide control of post-translational modifications

Nitric oxide (NO) is perfectly suited for the role of a redox signalling molecule. A key route for NO bioactivity occurs via protein S-nitrosation, and involves the addition of a NO moiety to a protein cysteine (Cys) thiol (–SH) to form an S-nitrosothiol (SNO). This process is thought to underpin a...

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Detalles Bibliográficos
Autores: Gupta, K. J., Kolbert, Z., Durner, J., Lindermayr, C., Corpas, Francisco J., Brouquisse, R., Barroso-Albarracín, Juan Bautista, Umbreen, S., Palma Martínez, José Manuel, Hancock, John T., Petřivalský, M., Wendehenne, D., Loake, G.J.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/218815
Acceso en línea:http://hdl.handle.net/10261/218815
Access Level:acceso abierto
Palabra clave:Nitric oxide (NO)
Persulfidation
Phosphorylation
Reactive nitrogen species( RNS)
Reactive oxygen species (ROS)
S-nitrosation
S-nitrosylation
SUMOylation
Descripción
Sumario:Nitric oxide (NO) is perfectly suited for the role of a redox signalling molecule. A key route for NO bioactivity occurs via protein S-nitrosation, and involves the addition of a NO moiety to a protein cysteine (Cys) thiol (–SH) to form an S-nitrosothiol (SNO). This process is thought to underpin a myriad of cellular processes in plants that are linked to development, environmental responses and immune function. Here we collate emerging evidence showing that NO bioactivity regulates a growing number of diverse post-translational modifications including SUMOylation, phosphorylation, persulfidation and acetylation. We provide examples of how NO orchestrates these processes to mediate plant adaptation to a variety of cellular cues.