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DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
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Single and double box HMGB proteins differentially destabilize nucleosomes.

Micah J McCauley1, Ran Huo1, Nicole Becker2

  • 1Department of Physics, Northeastern University, Boston, MA, USA.

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|November 17, 2018
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High mobility group B (HMGB) proteins like Hmo1 and Nhp6A disrupt nucleosomes, regulating chromatin accessibility. Hmo1 more extensively destabilizes nucleosomes than Nhp6A, explaining their distinct cellular roles.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Genetics

Background:

  • Nucleosome disruption is crucial for nuclear processes like transcription and DNA repair.
  • High mobility group B (HMGB) proteins are key regulators of chromatin structure and accessibility.

Purpose of the Study:

  • To investigate the mechanism by which HMGB proteins disrupt nucleosomes.
  • To elucidate the distinct roles of Hmo1 and Nhp6A in chromatin regulation.

Main Methods:

  • Combined atomic force microscopy (AFM) and optical tweezers (OT) experiments.
  • Analysis of high mobility group B (HMGB) protein interactions with nucleosomes.

Main Results:

  • Both Hmo1 and Nhp6A bind preferentially to nucleosomes over linker DNA.
  • HMGB proteins destabilize and unwind DNA from H2A-H2B dimers.
  • Hmo1 releases DNA from the (H3-H4)2 tetramer, unlike Nhp6A, indicating differential nucleosome disruption.

Conclusions:

  • HMGB proteins are potent nucleosome disruptors, offering a novel mechanism for chromatin accessibility control.
  • Differential nucleosome destabilization by Hmo1 and Nhp6A underlies their distinct genomic functions and cellular localization.