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TitleCODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 2181, Year 2025
Publish dateMar 4, 2025
AuthorsTae-Kyeong Jeong / R Ciaran MacKenzie Frater / Jongha Yoon / Anja Groth / Ji-Joon Song /
PubMed AbstractASF1 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 ...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.
External linksNat Commun / PubMed:40038274 / PubMed Central
MethodsEM (single particle)
Resolution3.75 Å
Structure data

60697

9imz

EMDB-60697, PDB-9imz:
CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate histone supply
Method: EM (single particle) / Resolution: 3.75 Å

Source
  • homo sapiens (human)
KeywordsREPLICATION / Histone chaperone / DNA replication / complex

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