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Structural determinants for generating centromeric chromatin.

Ben E Black1, Daniel R Foltz, Srinivas Chakravarthy

  • 1Ludwig Institute for Cancer Research, University of California, San Diego, La Jolla, California 92093, USA.

Nature
|July 30, 2004
PubMed
Summary
This summary is machine-generated.

Centromere identity is maintained by a unique histone variant, CENP-A (centromere protein A), which forms rigid nucleosomes. This structural property, conferred by CENP-A

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Area of Science:

  • Cell Biology
  • Epigenetics
  • Chromosomal Biology

Background:

  • Centromeres, crucial for chromosome segregation, lack defined DNA sequences in mammals.
  • Functional centromeres are characterized by the presence of CENP-A (centromere protein A), a histone H3 variant.

Purpose of the Study:

  • To investigate the structural properties of CENP-A containing nucleosomes.
  • To identify the structural basis for CENP-A's centromere targeting and function.

Main Methods:

  • Deuterium exchange/mass spectrometry
  • Hydrodynamic measures
  • Histone variant substitution experiments

Main Results:

  • CENP-A and histone H4 form more compact and rigid sub-nucleosomal tetramers compared to H3/H4 tetramers.
  • A specific domain in CENP-A is responsible for this compaction and rigidity.
  • Substituting this domain into histone H3 is sufficient to direct it to centromeres.

Conclusions:

  • The unique structural rigidity of CENP-A nucleosomes is conferred by a specific centromere-targeting domain.
  • This rigidity likely plays a critical role in establishing and maintaining centromere identity.
  • CENP-A's structural properties are key to its function in ensuring proper chromosome segregation.