CENP-A and CENP-B collaborate to create an open centromeric chromatin state
Harsh Nagpal,
Ahmad Ali-Ahmad,
Yasuhiro Hirano,
Wei Cai,
Mario Halic,
Tatsuo Fukagawa,
Nikolina Sekulić () and
Beat Fierz ()
Additional contact information
Harsh Nagpal: SB ISIC LCBM
Ahmad Ali-Ahmad: University of Oslo
Yasuhiro Hirano: Osaka University
Wei Cai: SB ISIC LCBM
Mario Halic: St. Jude Children’s Research Hospital
Tatsuo Fukagawa: Osaka University
Nikolina Sekulić: University of Oslo
Beat Fierz: SB ISIC LCBM
Nature Communications, 2023, vol. 14, issue 1, 1-18
Abstract:
Abstract Centromeres are epigenetically defined via the presence of the histone H3 variant CENP-A. Contacting CENP-A nucleosomes, the constitutive centromere associated network (CCAN) and the kinetochore assemble, connecting the centromere to spindle microtubules during cell division. The DNA-binding centromeric protein CENP-B is involved in maintaining centromere stability and, together with CENP-A, shapes the centromeric chromatin state. The nanoscale organization of centromeric chromatin is not well understood. Here, we use single-molecule fluorescence and cryoelectron microscopy (cryoEM) to show that CENP-A incorporation establishes a dynamic and open chromatin state. The increased dynamics of CENP-A chromatin create an opening for CENP-B DNA access. In turn, bound CENP-B further opens the chromatin fiber structure and induces nucleosomal DNA unwrapping. Finally, removal of CENP-A increases CENP-B mobility in cells. Together, our studies show that the two centromere-specific proteins collaborate to reshape chromatin structure, enabling the binding of centromeric factors and establishing a centromeric chromatin state.
Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43739-5
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DOI: 10.1038/s41467-023-43739-5
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