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Updated: Jul 8, 2025
05:35
Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
Published on: March 3, 2016
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CENP-A and CENP-B collaborate to create an open centromeric chromatin state
Harsh Nagpal1, Ahmad Ali-Ahmad2, Yasuhiro Hirano3
1École Polytechnique Fédérale de Lausanne (EPFL), SB ISIC LCBM, Station 6, CH-1015, Lausanne, Switzerland.
Nature Communications
|December 12, 2023
Summary
Centromere proteins CENP-A and CENP-B work together to create a dynamic, open chromatin structure. This collaboration is essential for centromere function and cell division.
Area of Science:
- Cell Biology
- Epigenetics
- Chromatin Structure
Background:
- Centromeres are crucial for cell division, defined epigenetically by CENP-A.
- The constitutive centromere-associated network (CCAN) and kinetochore assemble on CENP-A nucleosomes.
- CENP-B, a DNA-binding protein, contributes to centromere stability and chromatin state.
Purpose of the Study:
- To investigate the nanoscale organization of centromeric chromatin.
- To understand the interplay between CENP-A and CENP-B in shaping centromeric chromatin.
Main Methods:
- Single-molecule fluorescence microscopy
- Cryo-electron microscopy (cryoEM)
Main Results:
- CENP-A incorporation leads to a dynamic and open chromatin state.
- This open chromatin facilitates CENP-B DNA access and binding.
- CENP-B binding further opens chromatin and unwraps nucleosomal DNA.
- CENP-A removal increases CENP-B mobility.
Conclusions:
- CENP-A and CENP-B collaborate to reshape centromeric chromatin structure.
- This dynamic chromatin state enables the binding of essential centromeric factors.
- Their interaction establishes the unique epigenetic state of the centromere.
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