Nanotransducers in cellular redox signaling: modification of thiols by reactive oxygen and nitrogen species.
The control of signal transduction involves post-translational modification of proteins at key amino acids. Cysteine residues are important in the control of 'redox' cell-signaling pathways, as thiol chemistry offers the possibility of modification by structurally diverse species, including those derived from oxidized lipids, peroxides or nitric oxide. An important and provocative study of the modification of thiols in the transcription factor OxyR recently extended this hypothesis. The findings offer the enticing possibility that the cell can distinguish between different degrees of oxidant and nitrosative exposure by modification at a single site on a signaling molecule.
D000818:Animals; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism; D026361:Reactive Nitrogen Species / Q000009:adverse effects / Q000378:metabolism*; D017382:Reactive Oxygen Species / Q000009:adverse effects / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000378:metabolism*
D011506:Proteins; D026361:Reactive Nitrogen Species; D017382:Reactive Oxygen Species; D013438:Sulfhydryl Compounds; D003545:Cysteine