Cross-regulation of histone modifications

Nat Struct Mol Biol. 2007 Nov;14(11):1017-24. doi: 10.1038/nsmb1307. Epub 2007 Nov 5.


Histones undergo several different post-translational modifications that control a variety of physiological processes. These covalent modifications show substantial cross-regulation, providing a wealth of regulatory potential. New insights into the communication between modifications on histones have emerged in recent years. This review assesses the current understanding of cross-regulation of histone modifications and identifies future questions to be addressed in this field.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Histone Code*
  • Histones / metabolism*
  • Histones / physiology
  • Mass Spectrometry
  • Mitosis / genetics
  • Molecular Sequence Data
  • Protein Processing, Post-Translational / physiology*
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / metabolism


  • Histones
  • Tumor Suppressor Protein p53