Molecular basis for the redox control of nuclear transport of the structural chromatin protein Hmgb1.

@article{Hoppe2006MolecularBF,
  title={Molecular basis for the redox control of nuclear transport of the structural chromatin protein Hmgb1.},
  author={George Hoppe and Katherine E Talcott and Sanjoy K Bhattacharya and John W. Crabb and Jonathan E. Sears},
  journal={Experimental cell research},
  year={2006},
  volume={312 18},
  pages={3526-38}
}
Oxidative stress can induce a covalent disulfide bond between protein and peptide thiols that is reversible through enzymatic catalysis. This process provides a post-translational mechanism for control of protein function and may also protect thiol groups from irreversible oxidation. High mobility group protein B1 (Hmgb1), a DNA-binding structural chromosomal protein and transcriptional co-activator was identified as a substrate of glutaredoxin. Hmgb1 contains 3 cysteines, Cys23, 45, and 106… CONTINUE READING