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Related Concept Videos

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...
Nucleosome Remodeling02:54

Nucleosome Remodeling

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.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Heterochromatin02:38

Heterochromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Euchromatin01:01

Euchromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
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...
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...

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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

CENP-A-containing nucleosomes: easier disassembly versus exclusive centromeric localization.

Natalia Conde e Silva1, Ben E Black, Andrei Sivolob

  • 1Institut Jacques Monod (UMR CNRS 7592), 2 place Jussieu, 75251 Paris Cédex 05, France.

Journal of Molecular Biology
|May 26, 2007
PubMed
Summary

Centromere protein A (CENP-A) nucleosomes exhibit unique DNA unwrapping and easier disassembly compared to standard histone H3 nucleosomes. This suggests CENP-A

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Centromeric chromatin is essential for chromosome segregation during cell division.
  • CENP-A (centromere protein A) is a histone H3 variant crucial for centromere identity.
  • Understanding CENP-A nucleosome structure and dynamics is key to centromere function.

Purpose of the Study:

  • To investigate the structural and dynamic properties of CENP-A nucleosomes compared to canonical H3 nucleosomes.
  • To quantify DNA unwrapping and assess the stability and disassembly characteristics of CENP-A nucleosomes.

Main Methods:

  • Nucleosome reconstitution assays using CENP-A and H3 on various DNA templates (5S DNA, alpha-satellite DNA, minicircles).
  • Electrophoretic mobility comparisons to assess nucleosome positioning and DNA unwrapping.
  • Enzymatic assays (exonuclease III) and biochemical assays (linker histone binding, NAP-1 mediated dimer release, heparin-induced destabilization) to probe nucleosome dynamics.

Main Results:

  • CENP-A nucleosomes exhibit distinct DNA entry-exit unwrapping (approx. 7 bp) compared to H3 nucleosomes.
  • This unwrapping facilitates exonuclease III invasion but hinders linker histone binding.
  • CENP-A nucleosomes and (CENP-A-H4)2 tetramers show increased instability and easier disassembly than their H3 counterparts.

Conclusions:

  • CENP-A nucleosomes possess unique structural features, including DNA unwrapping and enhanced disassembly.
  • These properties likely facilitate the dynamic regulation of centromeric chromatin, enabling proper assembly and clearance.
  • The findings provide insights into the specialized role of CENP-A in establishing and maintaining centromere function.