Tae-Kyeong Jeong
@tkjeong.bsky.social
If you’d like to learn more, plz check out the link below. Hope you enjoy reading it! 😄
www.nature.com/articles/s41...
www.nature.com/articles/s41...
CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply - Nature Communications
CODANIN-1 negatively regulates the function of ASF1, the key chaperone for histone H3-H4 supply. Here the authors present the cryo-EM structure of the CODANIN-1_ASF1A complex, showing that CODANIN-1 u...
www.nature.com
March 7, 2025 at 4:21 PM
If you’d like to learn more, plz check out the link below. Hope you enjoy reading it! 😄
www.nature.com/articles/s41...
www.nature.com/articles/s41...
Furthermore, our structural and biochemical analyses, combined with in-cell studies, demonstrate that the dual-binding mode of CODANIN-1 and ASF1 is essential for the efficient cytoplasmic sequestration of ASF1.
March 7, 2025 at 4:21 PM
Furthermore, our structural and biochemical analyses, combined with in-cell studies, demonstrate that the dual-binding mode of CODANIN-1 and ASF1 is essential for the efficient cytoplasmic sequestration of ASF1.
This structural feature provides direct evidence that CODANIN-1 competes with histone H3/H4 for ASF1 binding. Such competition suggests that CODANIN-1 functions as a negative regulator of DNA replication by interfering with the formation of the histone H3/H4–ASF1 complex.
March 7, 2025 at 4:21 PM
This structural feature provides direct evidence that CODANIN-1 competes with histone H3/H4 for ASF1 binding. Such competition suggests that CODANIN-1 functions as a negative regulator of DNA replication by interfering with the formation of the histone H3/H4–ASF1 complex.
Interestingly, in addition to the previously known ASF1 binding motif of CODANIN-1, we identified novel binding motifs. Among them, the discovery of binding motifs that mimic the histone H3 helix was particularly striking. We named these helices the histone mimic helices (HMHs).
March 7, 2025 at 4:21 PM
Interestingly, in addition to the previously known ASF1 binding motif of CODANIN-1, we identified novel binding motifs. Among them, the discovery of binding motifs that mimic the histone H3 helix was particularly striking. We named these helices the histone mimic helices (HMHs).
Our study reveals the molecular mechanism of ASF1 cytoplasmic sequestration by CODANIN-1 based on the cryo-EM structure of the CODANIN-1_ASF1A complex. In our structure, CODANIN-1 exists as a dimer, with each CODANIN-1 monomer binding to two ASF1A molecules to form the complex.
March 7, 2025 at 4:21 PM
Our study reveals the molecular mechanism of ASF1 cytoplasmic sequestration by CODANIN-1 based on the cryo-EM structure of the CODANIN-1_ASF1A complex. In our structure, CODANIN-1 exists as a dimer, with each CODANIN-1 monomer binding to two ASF1A molecules to form the complex.