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Nucleosome structural changes due to acetylation

W R Bauer1, J J Hayes, J H White

  • 1Department of Microbiology, State University of New York, Stony Brook 11794-5222.

Journal of Molecular Biology
|February 25, 1994
PubMed
Summary
This summary is machine-generated.

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Histone acetylation does not alter the helical repeat of nucleosome-bound DNA. However, acetylation changes nucleosome shape, reducing DNA winding around the central axis, impacting DNA accessibility.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Structural Biology

Background:

  • Nucleosomes are the fundamental units of DNA packaging in eukaryotes.
  • Histone acetylation is a key epigenetic modification influencing gene regulation.
  • The precise structural impact of acetylation on nucleosome helical repeat remains debated.

Purpose of the Study:

  • To investigate the effect of histone acetylation on the helical repeat of nucleosome-bound DNA.
  • To determine if acetylation alters DNA-protein contacts within the nucleosome.
  • To analyze structural changes in acetylated nucleosomes using surface linking theory.

Main Methods:

  • Reconstitution of nucleosomes with HeLa cell histone octamers and Xenopus borealis 5S RNA gene DNA.
  • Hydroxyl radical footprinting to assess DNA-protein contacts and helical repeat.

Related Experiment Videos

  • Analysis using surface linking theory and existing minichromosome data.

    • Main Results:

    • Acetylation of nucleosomes did not change the helical repeat of the DNA.
    • The extent of DNA-protein contacts remained unaltered after acetylation.
    • Nucleosome shape changes upon acetylation, leading to decreased DNA winding.

    Conclusions:

    • Histone acetylation does not alter the intrinsic helical repeat of DNA within the nucleosome.
    • Acetylation-induced changes in nucleosome shape reduce DNA supercoiling.
    • These findings provide insights into how epigenetic modifications regulate DNA accessibility and gene expression.