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Related Concept Videos

The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
The Nucleosome01:19

The Nucleosome

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.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...

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Related Experiment Video

Updated: Jul 20, 2026

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
05:35

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins

Published on: March 3, 2016

Histone-histone interactions and centromere function.

L Glowczewski1, P Yang, T Kalashnikova

  • 1Department of Microbiology and Cancer Center, University of Virginia, Charlottesville, Virginia 22908, USA.

Molecular and Cellular Biology
|July 13, 2000
PubMed
Summary

The study confirms that Cse4p and histone H4 interact to form centromere nucleosomes in yeast. This interaction is crucial for proper chromosome segregation and centromere function.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Cse4p is a specialized histone H3 variant essential for centromere structure and function in Saccharomyces cerevisiae.
  • Histone H4 mutations (hhf1-20) cause defects in centromere chromatin and chromosome transmission.
  • A model proposes Cse4p and histone H4 interact via their histone fold domains to form centromeric nucleosomes.

Purpose of the Study:

  • To genetically test the proposed interaction between Cse4p and histone H4.
  • To identify specific regions of Cse4p involved in this interaction.
  • To investigate the role of histone H3 in centromere assembly.

Main Methods:

  • Targeted random mutagenesis of the Cse4p histone fold domain.
  • Isolation and characterization of temperature-sensitive cse4 alleles.
  • Genetic analysis including allele-specific suppression and dosage lethality experiments.

Main Results:

  • Three temperature-sensitive cse4 alleles were identified, two with mutations at the Cse4p-H4 interface, one showing long-range cooperative effects.
  • A third allele had mutations in the helix 2-helix 3 interface, important for H3 dimerization.
  • Reciprocal allele-specific suppression between Cse4p and histone H4 overexpression confirmed their interaction.
  • Histone H3 overexpression was lethal in cse4 mutants, indicating competition for histone H4.

Conclusions:

  • The results provide strong genetic evidence for a direct Cse4p-histone H4 interaction in centromere assembly.
  • Centromere chromatin assembly is a highly regulated process, evidenced by the pathway's resistance to histone H3 interference.
  • Understanding Cse4p-H4 interactions is key to comprehending centromere structure and epigenetic inheritance.