CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply

Tae-Kyeong Jeong, R. Ciaran MacKenzie Frater, Jongha Yoon, Anja Groth () and Ji-Joon Song ()
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Tae-Kyeong Jeong: Korea Advanced Institute of Science and Technology (KAIST)
R. Ciaran MacKenzie Frater: University of Copenhagen
Jongha Yoon: Korea Advanced Institute of Science and Technology (KAIST)
Anja Groth: University of Copenhagen
Ji-Joon Song: Korea Advanced Institute of Science and Technology (KAIST)

Nature Communications, 2025, vol. 16, issue 1, 1-17

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-56976-7

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