Single-molecule nucleosome remodeling by INO80 and effects of histone tails

FEBS Lett. 2018 Feb;592(3):318-331. doi: 10.1002/1873-3468.12973. Epub 2018 Jan 26.

Abstract

Genome maintenance and integrity requires continuous alterations of the compaction state of the chromatin structure. Chromatin remodelers, among others the INO80 complex, help organize chromatin by repositioning, reshaping, or evicting nucleosomes. We report on INO80 nucleosome remodeling, assayed by single-molecule Foerster resonance energy transfer on canonical nucleosomes as well as nucleosomes assembled from tailless histones. Nucleosome repositioning by INO80 is a processively catalyzed reaction. During the initiation of remodeling, probed by the INO80 bound state, the nucleosome reveals structurally heterogeneous states for tailless nucleosomes (in contrast to wild-type nucleosomes). We, therefore, propose an altered energy landscape for the INO80-mediated nucleosome sliding reaction in the absence of histone tails.

Keywords: chromatin remodeling; nucleosome; single-molecule FRET.

Publication types

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

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Adenosine Diphosphate / metabolism
  • Chromatin / metabolism
  • Chromatin Assembly and Disassembly
  • DNA / metabolism
  • DNA Helicases / metabolism*
  • DNA-Binding Proteins
  • Histones / metabolism*
  • Humans
  • Models, Molecular
  • Nucleosomes / metabolism*
  • Single Molecule Imaging / methods*

Substances

  • Chromatin
  • DNA-Binding Proteins
  • Histones
  • Nucleosomes
  • Adenosine Diphosphate
  • DNA
  • ATPases Associated with Diverse Cellular Activities
  • DNA Helicases
  • INO80 protein, human