Article
Specific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non-functional apoptosome
Author/s | 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 |
Department | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular |
Publication Date | 2012 |
Deposit Date | 2018-03-06 |
Published in |
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Abstract | 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 ... 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. |
Project ID. | 10.1016/j.febslet.2011.12.007 |
Citation | 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. |
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