Structural basis for H2A-H2B recognitions by human Spt16

Biochem Biophys Res Commun. 2023 Apr 9:651:85-91. doi: 10.1016/j.bbrc.2023.02.016. Epub 2023 Feb 10.

Abstract

The human facilitates chromatin transcription (FACT) complex, consisting of Spt16 and SSRP1, is a versatile histone chaperone that can engage free H2A-H2B dimer and H3-H4 tetramer (or dimer), and partially unraveled nucleosome. The C-terminal domain of human Spt16 (hSpt16-CTD) is the decisive element for engaging H2A-H2B dimer and partially unraveled nucleosome. The molecular basis of the H2A-H2B dimer recognitions by hSpt16-CTD is not fully comprehended. Here, we present a high-resolution snapshot of the recognitions of the H2A-H2B dimer by hSpt16-CTD via an acidic intrinsically disordered (AID) segment, and reveal some distinct structural features of hSpt16-CTD as compared to the budding yeast Spt16-CTD.

Keywords: Crystal structure; Histone chaperone; Spt16.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA-Binding Proteins
  • High Mobility Group Proteins
  • Histone Chaperones
  • Histones* / metabolism
  • Humans
  • Nucleosomes*
  • Protein Binding
  • Transcriptional Elongation Factors

Substances

  • DNA-Binding Proteins
  • High Mobility Group Proteins
  • Histone Chaperones
  • Histones
  • Nucleosomes
  • SSRP1 protein, human
  • Transcriptional Elongation Factors
  • SUPT16H protein, human