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CFP1 Regulates Histone H3K4 Trimethylation and Developmental Potential in Mouse Oocytes.

Abstract：

:Trimethylation of histone H3 at lysine-4 (H3K4me3) is associated with eukaryotic gene promoters and poises their transcriptional activation during development. To examine the in vivo function of H3K4me3 in the absence of DNA replication, we deleted CXXC finger protein 1 (CFP1), the DNA-binding subunit of the SETD1 histone H3K4 methyltransferase, in developing oocytes. We find that CFP1 is required for H3K4me3 accumulation and the deposition of histone variants onto chromatin during oocyte maturation. Decreased H3K4me3 in oocytes caused global downregulation of transcription activity. Oocytes lacking CFP1 failed to complete maturation and were unable to gain developmental competence after fertilization, due to defects in cytoplasmic lattice formation, meiotic division, and maternal-zygotic transition. Our study highlights the importance of H3K4me3 in continuous histone replacement for transcriptional regulation, chromatin remodeling, and normal developmental progression in a non-replicative system.

journal_name

Cell Rep

journal_title

Cell reports

authors

Yu C,Fan X,Sha QQ,Wang HH,Li BT,Dai XX,Shen L,Liu J,Wang L,Liu K,Tang F,Fan HY

doi

10.1016/j.celrep.2017.07.011

subject

Has Abstract

pub_date

2017-08-01 00:00:00

pages

1161-1172

issue

5

issn

2211-1247

pii

S2211-1247(17)30964-6

journal_volume

20

pub_type

杂志文章

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