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Article: CFP1 Regulates Histone H3K4 Trimethylation and Developmental Potential in Mouse Oocytes

TitleCFP1 Regulates Histone H3K4 Trimethylation and Developmental Potential in Mouse Oocytes
Authors
KeywordsCxxC1 finger protein 1
zygotic genome activation
oocyte
maternal-zygotic transition
histone H3K4 trimethylation
histone exchange
female fertility
Issue Date2017
Citation
Cell Reports, 2017, v. 20, n. 5, p. 1161-1172 How to Cite?
Abstract© 2017 The Authors 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.
Persistent Identifierhttp://hdl.handle.net/10722/265714
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYu, Chao-
dc.contributor.authorFan, Xiaoying-
dc.contributor.authorSha, Qian Qian-
dc.contributor.authorWang, Hui Han-
dc.contributor.authorLi, Bo Tai-
dc.contributor.authorDai, Xing Xing-
dc.contributor.authorShen, Li-
dc.contributor.authorLiu, Junping-
dc.contributor.authorWang, Lie-
dc.contributor.authorLiu, Kui-
dc.contributor.authorTang, Fuchou-
dc.contributor.authorFan, Heng Yu-
dc.date.accessioned2018-12-03T01:21:28Z-
dc.date.available2018-12-03T01:21:28Z-
dc.date.issued2017-
dc.identifier.citationCell Reports, 2017, v. 20, n. 5, p. 1161-1172-
dc.identifier.urihttp://hdl.handle.net/10722/265714-
dc.description.abstract© 2017 The Authors 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.-
dc.languageeng-
dc.relation.ispartofCell Reports-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectCxxC1 finger protein 1-
dc.subjectzygotic genome activation-
dc.subjectoocyte-
dc.subjectmaternal-zygotic transition-
dc.subjecthistone H3K4 trimethylation-
dc.subjecthistone exchange-
dc.subjectfemale fertility-
dc.titleCFP1 Regulates Histone H3K4 Trimethylation and Developmental Potential in Mouse Oocytes-
dc.typeArticle-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1016/j.celrep.2017.07.011-
dc.identifier.pmid28768200-
dc.identifier.scopuseid_2-s2.0-85026858286-
dc.identifier.volume20-
dc.identifier.issue5-
dc.identifier.spage1161-
dc.identifier.epage1172-
dc.identifier.eissn2211-1247-
dc.identifier.isiWOS:000406680000013-

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