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Nitric oxide as a regulator of gene expression: Studies with the transcription factor proteins cJun and p50
Author(s) -
PinedaMolina Estela,
Lamas Santiago
Publication year - 2001
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.5520150213
Subject(s) - s nitrosylation , cysteine , chemistry , transcription factor , glutathione , transcription (linguistics) , oxidative phosphorylation , dna binding protein , biochemistry , covalent bond , nitrosylation , dna , redox , s nitrosoglutathione , nitric oxide , cysteine metabolism , regulator , gene expression , microbiology and biotechnology , gene , biology , enzyme , inorganic chemistry , organic chemistry , linguistics , philosophy
Both oxidative and nitrosative stresses may result in the inactivation of the binding to DNA of redox‐sensitive transcription factors. The underlying biochemical mechanisms may involve oxidation or nitrosylation of critical thiols within the DNA binding domains of these proteins. However, S‐glutahionylation, the formation of a mixed disulfide between glutathione and the redox‐sensitive cysteine residues, has been shown to occur under NO exposure and pro‐oxidative conditions in c‐Jun, one of the AP‐1 constituents [1,2]. This modification may be functionally important as it is reversible and has been detected in other transcription factors, such as NF‐κ, by using covalent chromatography with a modified S‐nitrosoglutathione sepharose [3].