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Título: | Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation |
Autor: | Klatt, Peter CSIC; Pineda-Molina, Estela CSIC ORCID; Lamas Peláez, Santiago CSIC ORCID | Palabras clave: | NF-kappa-b Redox regulation Nitrosative stress Serum-albumin Sulfenic acid In-vitro Thiols AP-1 Nitrosoglutathione Transcription |
Fecha de publicación: | 28-may-1999 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | J Biol Chem 274(22):15857-64 (1999) | Resumen: | This study addresses potential molecular mechanisms underlying the inhibition of the transcription factor c-Jun by nitric oxide. We show that in the presence of the physiological sulfhydryl glutathione nitric oxide modifies the two cysteine residues contained in the DNA binding module of c-Jun in a selective and distinct way. Although nitric oxide induced the formation of an intermolecular disulfide bridge between cysteine residues in the leucine zipper site of c-Jun monomers, this same radical directed the covalent incorporation of stoichiometric amounts of glutathione to a single conserved cysteine residue in the DNA-binding site of the protein. We found that covalent dimerization of c-Jun apparently did not affect its DNA binding activity, whereas the formation of a mixed disulfide with glutathione correlated well with the inhibition of transcription factor binding to DNA. Furthermore, we provide experimental evidence that nitric oxide-induced S-glutathionylation and inhibition of c-Jun involves the formation of S-nitrosoglutathione. In conclusion, our results support the reversible formation of a mixed disulfide between glutathione and c-Jun as a potential mechanism by which nitrosative stress may be transduced into a functional response at the level of transcription. | Descripción: | 9 p.-8 fig.-1 tab. | Versión del editor: | https://doi.org/10.1074/jbc.274.22.15857 | URI: | http://hdl.handle.net/10261/169823 | DOI: | 10.1074/jbc.274.22.15857 | ISSN: | 0021-9258 | E-ISSN: | 1083-351X |
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J. Biol. Chem.-1999-Klatt-15857-64.pdf | Artículo principal | 183,87 kB | Adobe PDF | Visualizar/Abrir |
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