Repositorio de producción científica de la Universidad de Sevilla

Specific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non-functional apoptosome

Opened Access Specific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non-functional apoptosome

Citas

buscar en

Estadísticas
Icon
Exportar a
Autor: García Heredia, José Manuel
Díaz Moreno, Irene
Díaz Quintana, Antonio Jesús
Orzáez, Mar
Navarro Carruesco, José Antonio
Hervás Morón, Manuel
Rosa Acosta, Miguel Ángel de la
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2012
Publicado en: FEBS Letters, 586, 154-158.
Tipo de documento: Artículo
Resumen: Under nitroxidative stress, a minor fraction of cytochrome c can be modified by tyrosine nitration. Here we analyze the specific effect of nitration of tyrosines 46 and 48 on the dual role of cytochrome c in cell survival and cell death. Our findings reveal that nitration of these two solvent-exposed residues has a negligible effect on the rate of electron transfer from cytochrome c to cytochrome c oxidase, but impairs the ability of the heme protein to activate caspase-9 by assembling a non-functional apoptosome. It seems that cytochrome c nitration under cellular stress counteracts apoptosis in light of the small amount of modified protein. We conclude that other changes such as increased peroxidase activity prevail and allow the execution of apoptosis.
Cita: García Heredia, J.M., Díaz Moreno, I., Díaz Quintana, A., Orzáez, M., Navarro Carruesco, J.A., Hervás Morón, M. y Rosa Acosta, M.Á.d.l. (2012). Specific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non-functional apoptosome. FEBS Letters, 586, 154-158.
Tamaño: 403.4Kb
Formato: PDF

URI: https://hdl.handle.net/11441/70835

DOI: 10.1016/j.febslet.2011.12.007

Ver versión del editor

Mostrar el registro completo del ítem


Esta obra está bajo una Licencia Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 Internacional

Este registro aparece en las siguientes colecciones