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Related Experiment Videos

Nucleosome core particles containing a poly(dA.dT) sequence element exhibit a locally distorted DNA structure.

Yunhe Bao1, Cindy L White, Karolin Luger

  • 1Howard Hughes Medical Institute and Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA.

Journal of Molecular Biology
|July 25, 2006
PubMed
Summary

Poly(dA.dT) DNA elements in nucleosomes increase stability against histone octamer sliding. These findings explain modest increases in DNA accessibility and transcription levels observed in vivo.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Poly(dA.dT) DNA sequences are implicated in transcriptional regulation.
  • These elements may influence nucleosome stability and DNA accessibility.
  • Understanding nucleosome dynamics is crucial for gene expression control.

Purpose of the Study:

  • To investigate the stability and structure of nucleosome core particles containing a poly(dA.dT) DNA element.
  • To determine how the poly(dA.dT) sequence affects histone octamer sliding and DNA-histone interactions.
  • To elucidate the structural basis for the functional role of poly(dA.dT) elements in nucleosomes.

Main Methods:

  • In vitro histone octamer sliding assays.
  • Fluorescence resonance energy transfer (FRET) to study DNA-histone interactions.

Related Experiment Videos

  • X-ray crystallography to determine the high-resolution structure of the nucleosome core particle.

    • Main Results:

    • Nucleosomes with a 16 base-pair poly(dA.dT) element (A16 NCP) exhibit increased thermal stability against histone octamer sliding.
    • Fluorescence resonance energy transfer revealed destabilized interactions between nucleosomal DNA ends and the histone octamer in A16 NCP.
    • The crystal structure of A16 NCP showed overall structural integrity with localized DNA conformational deviations.

    Conclusions:

    • Poly(dA.dT) elements enhance nucleosome stability, requiring higher temperatures for histone octamer repositioning.
    • Destabilized DNA-histone interactions at the nucleosome ends contribute to altered nucleosome dynamics.
    • The structural and dynamic changes induced by poly(dA.dT) elements are consistent with modest increases in DNA accessibility and transcription.