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Related Experiment Videos

Linker histone-dependent DNA structure in linear mononucleosomes

A Hamiche1, P Schultz, V Ramakrishnan

  • 1Institut Jacques Monod Centre National de la Recherche Scientifique et Université Paris, France.

Journal of Molecular Biology
|March 22, 1996
PubMed
Summary

Linker histone H5 (LH) binding to mononucleosomes alters DNA structure. The C-terminal tail of H5 forms a stem, bridging DNA ends and impacting chromatin fiber models.

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Area of Science:

  • Chromatin biology
  • Molecular genetics
  • Structural biology

Background:

  • Mononucleosomes are fundamental units of chromatin structure.
  • Linker histones, like histone H5 (H5), play crucial roles in higher-order chromatin organization.
  • Understanding histone-DNA interactions is key to deciphering gene regulation.

Purpose of the Study:

  • To investigate the binding of linker histone H5 to mononucleosomes.
  • To elucidate the structural consequences of H5 binding on DNA conformation within mononucleosomes.
  • To determine the role of the H5 C-terminal tail in modulating nucleosome structure.

Main Methods:

  • Reconstitution of mononucleosomes on short DNA fragments.
  • Electrophoretic mobility shift assays using engineered H5 variants.

Related Experiment Videos

  • Cryo-electron microscopy for high-resolution structural visualization.

    • Main Results:

    • Histone H5 binding alters the electrophoretic mobility of mononucleosomes.
    • The globular domain of H5 increases DNA wrapping but maintains uncrossed entry/exit DNA.
    • The H5 C-terminal tail forms a DNA stem structure, bridging entering and exiting DNA strands.

    Conclusions:

    • The C-terminal tail of linker histone H5 is critical for its interaction with mononucleosomes.
    • H5 binding influences DNA conformation, promoting a four-stranded DNA stem.
    • These findings provide insights into the structural basis of chromatin compaction and may constrain models of the 30 nm fiber.