CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply
Tallennettuna:
| Julkaisussa: | bioRxiv (Feb 7, 2025) |
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| Päätekijä: | |
| Muut tekijät: | , , , |
| Julkaistu: |
Cold Spring Harbor Laboratory Press
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| Aiheet: | |
| Linkit: | Citation/Abstract Full text outside of ProQuest |
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| LEADER | 00000nab a2200000uu 4500 | ||
|---|---|---|---|
| 001 | 3165216408 | ||
| 003 | UK-CbPIL | ||
| 022 | |a 2692-8205 | ||
| 024 | 7 | |a 10.1101/2024.07.10.602876 |2 doi | |
| 035 | |a 3165216408 | ||
| 045 | 0 | |b d20250207 | |
| 100 | 1 | |a Tae-Kyeong Jeong | |
| 245 | 1 | |a CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply | |
| 260 | |b Cold Spring Harbor Laboratory Press |c Feb 7, 2025 | ||
| 513 | |a Working Paper | ||
| 520 | 3 | |a 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 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 electron microscopy (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 a unique negative regulator that highjacks ASF1 interaction sites with histones and downstream chaperones to inhibit nucleosome assembly.Competing Interest StatementJ.S. is a CTO of Epinogen. A.G. is a co-founder and CSO of Ankrin Therapeutics.Footnotes* We included a new structure of the complex and its biochemical analysis | |
| 653 | |a Electron microscopy | ||
| 653 | |a Molecular modelling | ||
| 653 | |a Chromatin remodeling | ||
| 653 | |a DNA biosynthesis | ||
| 653 | |a Biochemical analysis | ||
| 653 | |a Cytoplasm | ||
| 653 | |a Structure-function relationships | ||
| 653 | |a Histone H3 | ||
| 653 | |a Histones | ||
| 653 | |a DNA structure | ||
| 700 | 1 | |a R Ciaran Mackenzie Frater | |
| 700 | 1 | |a Yoon, Jongha | |
| 700 | 1 | |a Groth, Anja | |
| 700 | 1 | |a Ji-Joon Song | |
| 773 | 0 | |t bioRxiv |g (Feb 7, 2025) | |
| 786 | 0 | |d ProQuest |t Biological Science Database | |
| 856 | 4 | 1 | |3 Citation/Abstract |u https://www.proquest.com/docview/3165216408/abstract/embedded/7BTGNMKEMPT1V9Z2?source=fedsrch |
| 856 | 4 | 0 | |3 Full text outside of ProQuest |u https://www.biorxiv.org/content/10.1101/2024.07.10.602876v2 |