Crystal structure of DPF3b in complex with an acetylated histone peptide

J Struct Biol. 2016 Sep;195(3):365-372. doi: 10.1016/j.jsb.2016.07.001. Epub 2016 Jul 16.

Abstract

Histone acetylation plays an important role in chromatin dynamics and is associated with active gene transcription. This modification is written by acetyltransferases, erased by histone deacetylases and read out by bromodomain containing proteins, and others such as tandem PHD fingers of DPF3b. Here we report the high resolution crystal structure of the tandem PHD fingers of DPF3b in complex with an H3K14ac peptide. In the complex structure, the histone peptide adopts an α-helical conformation, unlike previously observed by NMR, but similar to a previously reported MOZ-H3K14ac complex structure. Our crystal structure adds to existing evidence that points to the α-helix as a natural conformation of histone tails as they interact with histone-associated proteins.

Keywords: DPF3b; H3K14ac; Tandem PHD fingers; α-Helical conformation.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetylation
  • Crystallography, X-Ray
  • DNA-Binding Proteins / chemistry*
  • Histones / chemistry*
  • Humans
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • PHD Zinc Fingers
  • Peptide Fragments / chemistry
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Protein Interaction Domains and Motifs
  • Protein Processing, Post-Translational
  • Transcription Factors / chemistry*

Substances

  • DNA-Binding Proteins
  • DPF3 protein, human
  • Histones
  • Peptide Fragments
  • Transcription Factors