The synergy between RSC, Nap1 and adjacent nucleosome in nucleosome remodeling

Biochim Biophys Acta Gene Regul Mech. 2019 Feb;1862(2):129-140. doi: 10.1016/j.bbagrm.2018.11.008. Epub 2018 Dec 26.

Abstract

Eukaryotes have evolved a specific strategy to package DNA. The nucleosome is a 147-base-pair DNA segment wrapped around histone core proteins that plays important roles regulating DNA-dependent biosynthesis and gene expression. Chromatin remodeling complexes (RSC, Remodel the Structure of Chromatin) hydrolyze ATP to perturb DNA-histone contacts, leading to nucleosome sliding and ejection. Here, we utilized tethered particle motion (TPM) experiments to investigate the mechanism of RSC-mediated nucleosome remodeling in detail. We observed ATP-dependent RSC-mediated DNA looping and nucleosome ejection along individual mononucleosomes and dinucleosomes. We found that nucleosome assembly protein 1 (Nap1) enhanced RSC-mediated nucleosome ejection in a two-step disassembly manner from dinucleosomes but not from mononucleosomes. Based on this work, we provide an entire reaction scheme for the RSC-mediated nucleosome remodeling process that includes DNA looping, nucleosome ejection, the influence of adjacent nucleosomes, and the coordinated action between Nap1 and RSC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Chromatin Assembly and Disassembly*
  • DNA / metabolism
  • DNA-Binding Proteins / metabolism*
  • Eukaryota / genetics*
  • Histones / metabolism
  • Nucleosome Assembly Protein 1 / metabolism*
  • Nucleosomes / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcription Factors / metabolism*

Substances

  • DNA-Binding Proteins
  • Histones
  • NAP1 protein, S cerevisiae
  • Nucleosome Assembly Protein 1
  • Nucleosomes
  • RSC complex, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Adenosine Triphosphate
  • DNA