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Related Concept Videos

The Nucleosome Core Particle02:10

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination
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Structure of the Human Core Centromeric Nucleosome Complex.

Praveen Kumar Allu1, Jennine M Dawicki-McKenna1, Trevor Van Eeuwen2

  • 1Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA; Epigenetics Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

Current Biology : CB
|July 30, 2019
PubMed
Summary
This summary is machine-generated.

Centromeric nucleosome complexes (CCNC) with varying CENP-N amounts were structurally analyzed. These findings explain CENP-C specificity for CENP-A nucleosomes and how proteins interact at the chromosome-kinetochore interface during mitosis.

Keywords:
cell divisioncentromerechromatincryo-EMepigeneticshistonekinetochoremicrotubule spindlemitosisnucleosome

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Area of Science:

  • Molecular Biology
  • Chromatin Biology
  • Structural Biology

Background:

  • Centromeric nucleosomes are crucial for chromosome-kinetochore connections during mitosis.
  • The core centromeric nucleosome complex (CCNC) involves CENP-A, CENP-C, and CENP-N.
  • CENP-C interacts with nucleosomes via its central domain (CD) and CENP-C motif (CM).

Purpose of the Study:

  • To determine the structures of symmetric and asymmetric CCNC forms with varying CENP-N stoichiometry.
  • To elucidate the mechanism of CENP-C's specificity for CENP-A nucleosomes.
  • To understand how CCNC structure facilitates chromosome-kinetochore interactions in mitosis.

Main Methods:

  • X-ray crystallography to determine CCNC structures.
  • Analysis of protein-nucleosome interactions and stoichiometry.
  • Comparison with previous structural data and biological observations.

Main Results:

  • Identified a loss of one CENP-N for every two CENP-C copies in centromeric chromatin before kinetochore formation.
  • Presented structures of symmetric and asymmetric CCNC, revealing varying CENP-N stoichiometry.
  • Explained CENP-C's specific binding to CENP-A nucleosomes and the interaction of CENP-C/CENP-N with the histone H4 tail.

Conclusions:

  • The study explains the molecular basis for CENP-C's specificity and the structural organization of the CCNC.
  • Natural centromeric DNA paths support symmetric CCNC assembly surfaces.
  • Proposed that CCNC asymmetry in mitosis accommodates its role at the chromosome/kinetochore interface.