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Related Experiment Videos

Internal modifications in the CENP-A nucleosome modulate centromeric dynamics.

Minh Bui1, Mary Pitman1,2, Arthur Nuccio3

  • 1Chromatin Structure and Epigenetic Mechanisms Unit, Laboratory of Receptor Biology and Gene Expression, CCR, NCI, NIH, Bethesda, MD 20892 USA.

Epigenetics & Chromatin
|April 12, 2017
PubMed
Summary

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This summary is machine-generated.

Cyclical modifications of centromere histone CENP-A, specifically at lysine 124, regulate kinetochore protein binding and mitosis integrity. This study reveals a dynamic acetylation and methylation cycle influencing centromeric replication and chromosome segregation.

Area of Science:

  • Epigenetics and Chromatin Biology
  • Molecular Cell Biology
  • Genetics and Genomics

Background:

  • Posttranslational modifications (PTMs) of core histones regulate chromatin structure and gene expression.
  • PTMs of the centromere-specific histone H3 variant CENP-A are poorly understood, despite their potential roles in centromere function.
  • Lysine 124 (K124) of human CENP-A was previously identified as acetylated before DNA replication.

Purpose of the Study:

  • To investigate the functional significance of CENP-A K124 modifications.
  • To elucidate the role of CENP-A K124 acetylation and its dynamic changes in centromere function and mitosis.

Main Methods:

  • In silico computational modeling to predict structural effects of K124 acetylation.
  • In vivo studies using CENP-A mutants mimicking acetylation or unacetylation (K124Q, K124A).

Related Experiment Videos

  • Mass spectrometry to analyze CENP-A modifications during the cell cycle and identify associated enzymes.

    • Main Results:

    • Acetylation of CENP-A K124 was computationally shown to tighten the histone core, reduce C-terminus accessibility, and decrease CENP-C binding.
    • Nucleosomes with acetylated CENP-A K124 and H4 K79 were more prone to DNA sliding.
    • In vivo mutations of K124 altered CENP-C levels, increased mitotic errors, and affected centromeric replication timing.
    • CENP-A K124 undergoes cyclical modifications: acetylation at G1/S, switching to monomethylation during early and mid-S phases.
    • The histone acetyltransferase (HAT) p300 was implicated in the CENP-A K124 acetylation cycle.

    Conclusions:

    • Cyclical modifications of CENP-A, including K124 acetylation and subsequent methylation, are crucial for kinetochore protein binding and mitotic integrity.
    • These modifications influence centromeric replication timing and overall chromosome segregation fidelity.
    • The dynamic modification cycle of CENP-A highlights the importance of histone variant PTMs in fundamental biological processes.