Histone acetylation and deacetylation – Mechanistic insights from structural biology

Avinash B. Patel*, Yuan He, Ishwar Radhakrishnan

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Histones are subject to a diverse array of post-translational modifications. Among them, lysine acetylation is not only the most pervasive and dynamic modification but also highly consequential for regulating gene transcription. Although enzymes responsible for the addition and removal of acetyl groups were discovered almost 30 years ago, high-resolution structures of the enzymes in the context of their native complexes are only now beginning to become available, thanks to revolutionary technologies in protein structure determination and prediction. Here, we will review our current understanding of the molecular mechanisms of acetylation and deacetylation engendered by chromatin-modifying complexes, compare and contrast shared features, and discuss some of the pressing questions for future studies.

Original languageEnglish (US)
Article number147798
StatePublished - Jan 10 2024


  • Chromatin-modifying enzyme
  • Cryo-EM
  • Gene activation
  • HAT
  • HDAC
  • Histone acetylation
  • Histone deacetylation
  • Histone modification
  • Structural biology
  • Transcription activation
  • Transcription regulation
  • Transcription repression

ASJC Scopus subject areas

  • Genetics


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