NDLI: Nitric Oxide Inhibits c-Jun DNA Binding by Specifically TargetedS-Glutathionylation

Content Provider	Journal of Biological Chemistry (JBC)
Author	Klatt, Peter Molina, Estela Pineda Lamas, Santiago
Abstract	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-inducedS-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.
Related Links	http://www.jbc.org/content/274/22/15857.abstract
Ending Page	15864
Starting Page	15857
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	22
Volume Number	274
DOI	10.1074/jbc.274.22.15857
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1999-05-28
Access Restriction	Open
Subject Keyword	Nitric oxide (NO) 2,2-diethyl-1-nitroso-oxyhydrazine sodium salt (DEA/NO) S-nitrosoglutathione (GSNO) Dithiothreitol, AP-1, activator protein-1 (DTT) Wild type human c-Jun DNA binding domain (CC-Jun) Human c-Jun DNA binding domain with a cysteine 269 to serine mutation (SC-Jun) Human c-Jun DNA binding domain with a cysteine 320 to serine mutation (CS-Jun) Polyacrylamide gel electrophoresis (PAGE) Electrophoretic mobility shift assay (EMSA) PROTEIN CHEMISTRY AND STRUCTURE
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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