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TitleCENP-A and CENP-B collaborate to create an open centromeric chromatin state.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 8227, Year 2023
Publish dateDec 12, 2023
AuthorsHarsh Nagpal / Ahmad Ali-Ahmad / Yasuhiro Hirano / Wei Cai / Mario Halic / Tatsuo Fukagawa / Nikolina Sekulić / Beat Fierz /
PubMed AbstractCentromeres 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 ...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.
External linksNat Commun / PubMed:38086807 / PubMed Central
MethodsEM (single particle)
Resolution2.73 - 6.7 Å
Structure data

EMDB-18699: Human H3 nucleosome assembled on alpha-satellite DNA (Class1: most wrapped DNA)
Method: EM (single particle) / Resolution: 2.73 Å

EMDB-18714: Human H3 nucleosome assembled on alpha-satellite DNA (most unwrapped)
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-18739: Human CENP-A nucleosome assembled on alpha-satellite DNA (most wrapped DNA)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-18740: Human CENP-A nucleosome assembled on alpha-satellite DNA (partially unwrapped)
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-18745: Human Cenp-A nucleosome assembled on alpha-satellite DNA (most unwrapped DNA)
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-18753: Human CENP-A nucleosome assembled on alpha-satellite DNA in complex with CENP-B (most wrapped DNA)
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-18763: Human CENP-A nucleosome assembled on alpha-satellite DNA in complex with CENP-B (partially unwrapped DNA)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-18768: Human CENP-A nucleosome assembled on alpha-satellite DNA (most unwrapped DNA)
Method: EM (single particle) / Resolution: 6.7 Å

EMDB-18775: Human CENP-A nucleosome assembled on 601 DNA with CENP-B box
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-18776: Human CENP-A nucleosome assembled on 601 DNA with CENP-B box in complex with CENP-B
Method: EM (single particle) / Resolution: 3.2 Å

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  • Homo sapiens (human)
  • synthetic construct (others)

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