Atypical histone targets of PHD fingers

J Biol Chem. 2023 Apr;299(4):104601. doi: 10.1016/j.jbc.2023.104601. Epub 2023 Mar 11.

Abstract

Plant homeodomain (PHD) fingers are structurally conserved zinc fingers that selectively bind unmodified or methylated at lysine 4 histone H3 tails. This binding stabilizes transcription factors and chromatin-modifying proteins at specific genomic sites, which is required for vital cellular processes, including gene expression and DNA repair. Several PHD fingers have recently been shown to recognize other regions of H3 or histone H4. In this review, we detail molecular mechanisms and structural features of the noncanonical histone recognition, discuss biological implications of the atypical interactions, highlight therapeutic potential of PHD fingers, and compare inhibition strategies.

Keywords: PHD; binding; chromatin; histone; inhibitor.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • DNA-Binding Proteins / metabolism
  • Histones* / chemistry
  • Histones* / metabolism
  • Mice
  • Neoplasms / genetics
  • Neoplasms / physiopathology
  • PHD Zinc Fingers*
  • Protein Binding
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

  • DNA-Binding Proteins
  • Histones
  • Transcription Factors