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Related Concept Videos

Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Nucleosome Remodeling02:54

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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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The Nucleosome02:33

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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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The Nucleosome01:19

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Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can 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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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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Related Experiment Video

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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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An asymmetric centromeric nucleosome.

Yuichi Ichikawa1,2, Noriko Saitoh2, Paul D Kaufman1

  • 1Department of Molecular, Cell, and Cancer Biology, University of Massachusetts Medical School, Worcester, United States.

Elife
|August 24, 2018
PubMed
Summary
This summary is machine-generated.

Researchers created asymmetric histone H3 (centromeric H3/CENP-A) in yeast. A single extension is sufficient for kinetochore function, confirming the need for octameric centromeric nucleosomes for cell viability.

Keywords:
S. cerevisiaechromosomesgene expressionhistonekinetochorenucleosome

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Area of Science:

  • Chromatin biology
  • Molecular genetics
  • Cellular biology

Background:

  • Nucleosomes, fundamental DNA packaging units, possess a symmetric histone H3-H3 interface.
  • This inherent symmetry has limited understanding of nucleosome regulatory roles.
  • Previous work engineered asymmetric histone H3 dimers, enabling new research avenues.

Purpose of the Study:

  • To investigate the regulatory potential of nucleosome symmetry using an asymmetric histone H3 interface.
  • To adapt the asymmetric histone H3 system to the centromeric histone H3 variant (Cse4/CENP-A) in budding yeast.
  • To determine the functional requirements of centromeric nucleosome asymmetry for kinetochore function and cell viability.

Main Methods:

  • Molecular design and in vivo selection to generate obligately heterodimeric H3 proteins.
  • Application of this technique to the centromeric H3 isoform (Cse4/CENP-A) in Saccharomyces cerevisiae.
  • Analysis of kinetochore function and cell viability in yeast strains with engineered Cse4/CENP-A variants.

Main Results:

  • A single N- or C-terminal extension on Cse4/CENP-A is sufficient for essential kinetochore function.
  • The requirement for an octameric centromeric nucleosome for viability was validated.
  • The study demonstrates the broad applicability of the asymmetric H3 interface for chromatin research.

Conclusions:

  • Nucleosome symmetry is not strictly required for all centromeric functions.
  • Asymmetric histone interfaces provide a versatile tool for dissecting chromatin regulation.
  • The findings advance our understanding of centromere structure and function.