9IMZ
CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate histone supply
Summary for 9IMZ
| Entry DOI | 10.2210/pdb9imz/pdb |
| EMDB information | 60697 |
| Descriptor | Codanin-1, Histone chaperone ASF1A (2 entities in total) |
| Functional Keywords | histone chaperone, dna replication, complex, replication |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 330944.32 |
| Authors | Jeong, T.K.,Frater, R.C.M.,Yoon, J.,Groth, A.,Song, J.J. (deposition date: 2024-07-05, release date: 2025-03-19) |
| Primary citation | Jeong, T.K.,Frater, R.C.M.,Yoon, J.,Groth, A.,Song, J.J. CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply. Nat Commun, 16:2181-2181, 2025 Cited by PubMed Abstract: ASF1 is a major histone chaperone that regulates the supply of histone H3-H4 and facilitates nucleosome assembly to maintain chromatin structure during DNA replication and transcription. CODANIN-1 negatively regulates the function of ASF1. However, the molecular mechanism by which CODANIN-1 inhibits the ASF1-mediated histone supply remains elusive. Here, we present the cryo-EM structure of a human CODANIN-1_ASF1A complex at 3.75 Å resolution. The structure reveals that CODANIN-1 forms a dimer where each monomer holds two ASF1 molecules, utilizing two B-domains and two histone H3 mimic helices (HMHs). The interaction of CODANIN-1 with ASF1 via the HMH and B-domains inhibits the formation of an ASF1/H3-H4 complex and sequesters ASF1 in the cytoplasm. Our study provides a structural and molecular basis for the function of CODANIN-1 as negative regulator that highjacks ASF1 interaction sites with histones and downstream chaperones to inhibit nucleosome assembly. PubMed: 40038274DOI: 10.1038/s41467-025-56976-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.75 Å) |
Structure validation
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