Abstract:
:Trimethylation of histone H3 on lysine-4 (H3K4me3) is associated with gene-regulatory elements, but its transcription-independent function in cell division is unclear. CxxC-finger protein-1 (CFP1) is a major mediator of H3K4 trimethylation in mouse oocytes. Here we report that oocyte-specific knockout of Cxxc1, inhibition of CFP1 function, or abrogation of H3K4 methylation in oocytes each causes a delay of meiotic resumption as well as metaphase I arrest owing to defective spindle assembly and chromosome misalignment. These phenomena are partially attributed to insufficient phosphorylation of histone H3 at threonine-3. CDK1 triggers cell division-coupled degradation and inhibitory phosphorylation of CFP1. Preventing CFP1 degradation and phosphorylation causes CFP1 accumulation on chromosomes and impairs meiotic maturation and preimplantation embryo development. Therefore, CFP1-mediated H3K4 trimethylation provides 3a permission signal for the G2-M transition. Dual inhibition of CFP1 removes the SETD1-CFP1 complex from chromatin and ensures appropriate chromosome configuration changes during meiosis and mitosis.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Sha QQ,Dai XX,Jiang JC,Yu C,Jiang Y,Liu J,Ou XH,Zhang SY,Fan HYdoi
10.1038/s41467-018-05930-xsubject
Has Abstractpub_date
2018-08-28 00:00:00pages
3477issue
1issn
2041-1723pii
10.1038/s41467-018-05930-xjournal_volume
9pub_type
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