Oxidation of cysteine residues is a well-described means of sensing oxidative stress. Analysis of a bacterial transcriptional repressor protein indicates that metal-catalyzed oxidation of histidine residues can provide oxidative stress control in a cysteine-independent fashion.
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References
Lee, J.-W. & Helmann, J.D. Nature 440, 363–367 (2006).
Bsat, N., Herbig, A., Casillas-Martinez, L., Setlow, P. & Helmann, J.D. Mol. Microbiol. 29, 189–198 (1998).
Cadenas, E. Annu. Rev. Biochem. 58, 79–110 (1989).
Paget, M.S. & Buttner, M. Annu. Rev. Genet. 37, 91–121 (2003).
Little, J.W. Proc. Natl. Acad. Sci. USA 81, 1375–1379 (1984).
Kuge, S. & Jones, N. EMBO J. 13, 655–664 (1994).
Hantke, K. Curr. Opin. Microbiol. 4, 172–177 (2001).
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Moye-Rowley, W. Redox sensing and histidine oxidation: no longer PerR-fect strangers. Nat Chem Biol 2, 234–235 (2006). https://doi.org/10.1038/nchembio0506-234
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DOI: https://doi.org/10.1038/nchembio0506-234