RSC unravels the nucleosome

Mol Cell. 2001 Jan;7(1):89-95. doi: 10.1016/s1097-2765(01)00157-5.

Abstract

RSC and SWI/SNF chromatin-remodeling complexes were previously reported to generate a stably altered nucleosome. We now describe the formation of hybrids between nucleosomes of different sizes, showing that the stably altered structure is a noncovalent dimer. A basis for dimer formation is suggested by an effect of RSC on the supercoiling of closed, circular arrays of nucleosomes. The effect may be explained by the interaction of RSC with DNA at the ends of the nucleosome, which could lead to the release 60--80 bp or more from the ends. DNA released in this way may be trapped in the stable dimer or lead to alternative fates such as histone octamer transfer to another DNA or sliding along the same DNA molecule.

Publication types

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

MeSH terms

  • Animals
  • Chromatin / genetics
  • Chromatin / metabolism
  • DNA, Superhelical / chemistry
  • DNA, Superhelical / metabolism*
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / metabolism*
  • Dimerization
  • Drosophila Proteins*
  • Histones / genetics
  • Histones / metabolism
  • Nucleic Acid Conformation
  • Nucleosomes / chemistry
  • Nucleosomes / genetics*
  • Nucleosomes / metabolism*
  • RNA-Binding Proteins*
  • Rats
  • Ribonucleoprotein, U1 Small Nuclear / genetics
  • Ribonucleoprotein, U1 Small Nuclear / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism*
  • Xenopus laevis

Substances

  • Chromatin
  • DNA, Superhelical
  • DNA-Binding Proteins
  • Drosophila Proteins
  • Histones
  • Nucleosomes
  • RNA-Binding Proteins
  • RSC complex, S cerevisiae
  • Ribonucleoprotein, U1 Small Nuclear
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • snf protein, Drosophila