Nucleosome disruption by human SWI/SNF is maintained in the absence of continued ATP hydrolysis

J Biol Chem. 1996 Aug 23;271(34):20726-33. doi: 10.1074/jbc.271.34.20726.

Abstract

We have examined the requirement for ATP in human (h) SWI/SNF-mediated alteration of nucleosome structure and facilitation of transcription factor binding to nucleosomal DNA. hSWI/SNF-mediated nucleosome alteration requires hydrolysis of ATP or dATP. The alteration is stable upon removal of ATP from the reaction or upon inhibition of activity by excess ATPgammaS, indicating that continued ATP hydrolysis is not required to maintain the altered nucleosome structure. This stable alteration is sufficient to facilitate binding of a transcriptional activator protein; concurrent ATP hydrolysis was not required to facilitate binding. These data suggest sequential steps that can occur in the process by which transcription factors gain access to nucleosomal DNA.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / physiology*
  • Base Sequence
  • Consensus Sequence
  • DNA, Superhelical
  • DNA-Binding Proteins / metabolism
  • Drosophila Proteins*
  • Fungal Proteins / metabolism
  • HeLa Cells
  • Humans
  • Hydrolysis
  • Molecular Sequence Data
  • Nucleosomes / metabolism
  • Nucleosomes / ultrastructure*
  • Oligodeoxyribonucleotides / chemistry
  • Plasmids
  • RNA-Binding Proteins*
  • Ribonucleoprotein, U1 Small Nuclear / physiology*
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors / physiology*

Substances

  • DNA, Superhelical
  • DNA-Binding Proteins
  • Drosophila Proteins
  • Fungal Proteins
  • GAL4 protein, S cerevisiae
  • Nucleosomes
  • Oligodeoxyribonucleotides
  • RNA-Binding Proteins
  • Ribonucleoprotein, U1 Small Nuclear
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • snf protein, Drosophila
  • Adenosine Triphosphate