The cryo‐EM structure of the CENP‐A nucleosome in complex with ggKNL2
Abstract: Centromere protein A (CENP‐A) nucleosomes containing the centromere‐specific histone H3 variant CENP‐A represent an epigenetic mark that specifies centromere position. The Mis18 complex is a licensing factor for new CENP‐A deposition via the CENP‐A chaperone, Holliday junction recognition protein (HJURP), on the centromere chromatin. Chicken KINETOCHORE NULL2 (KNL2) (ggKNL2), a Mis18 complex component, has a CENP‐C‐like motif, and our previous study suggested that ggKNL2 directly binds to the CENP‐A nucleosome to recruit HJURP/CENP‐A to the centromere. However, the molecular basis for CENP‐A nucleosome recognition by ggKNL2 has remained unclear. Here, we present the cryo‐EM structure of the chicken CENP‐A nucleosome in complex with a ggKNL2 fragment containing the CENP‐C‐like motif. Chicken KNL2 distinguishes between CENP‐A and histone H3 in the nucleosome using the CENP‐C‐like motif and its downstream region. Both the C‐terminal tail and the RG‐loop of CENP‐A are simultaneously recognized as CENP‐A characteristics. The CENP‐A nucleosome–ggKNL2 interaction is thus essential for KNL2 functions. Furthermore, our structural, biochemical, and cell biology data indicate that ggKNL2 changes its binding partner at the centromere during chicken cell cycle progression.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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The cryo‐EM structure of the CENP‐A nucleosome in complex with ggKNL2 ; day:06 ; month:02 ; year:2023 ; extent:20
The EMBO journal / European Molecular Biology Organization ; (06.02.2023) (gesamt 20)
- Creator
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Jiang, Honghui
Ariyoshi, Mariko
Hori, Tetsuya
Watanabe, Reito
Makino, Fumiaki
Namba, Keiichi
Fukagawa, Tatsuo
- DOI
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10.15252/embj.2022111965
- URN
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urn:nbn:de:101:1-2023020614294362829435
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:57 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Jiang, Honghui
- Ariyoshi, Mariko
- Hori, Tetsuya
- Watanabe, Reito
- Makino, Fumiaki
- Namba, Keiichi
- Fukagawa, Tatsuo
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Cryo-EM structure of the SEA complex
Cryo-EM structure of the plant 26S proteasome
Cryo-EM structures of the human NLRP3 inflammasome
Statistical Inference of cryo-EM Maps
Functionalized graphene-oxide grids enable high-resolution cryo-EM structures of the SNF2h-nucleosome complex without crosslinking
Cryo-EM of the yeast mitochondrial ABC transporter Atm1
Prion strains viewed through the lens of cryo-EM
Architecture of the baculovirus nucleocapsid revealed by cryo-EM
Cryo-EM structures of the membrane repair protein dysferlin
Manifold methods for cryo-EM image denoising
Invariants for multireference alignment and cryo-EM
Cryo-EM of nucleosome core particle interactions in trans
Cryo-EM structure of the SEA complex
Cryo-EM structure of the plant 26S proteasome
Cryo-EM structures of the human NLRP3 inflammasome
Statistical Inference of cryo-EM Maps
Functionalized graphene-oxide grids enable high-resolution cryo-EM structures of the SNF2h-nucleosome complex without crosslinking
Cryo-EM of the yeast mitochondrial ABC transporter Atm1
Prion strains viewed through the lens of cryo-EM
Architecture of the baculovirus nucleocapsid revealed by cryo-EM
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