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PMID: 19078966 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Histone H3 lysine 4 trimethylation marks meiotic recombination initiation sites.

The EMBO journal ·Vol. 28 ·No. 2 ·2009-01-21 ·Pages 99-111

Borde V, Robine N, Lin W, Bonfils S, Géli V, Nicolas A

Abstract

The function of histone modifications in initiating and regulating the chromosomal events of the meiotic prophase remains poorly understood. In Saccharomyces cerevisiae, we examined the genome-wide localization of histone H3 lysine 4 trimethylation (H3K4me3) along meiosis and its relationship to gene expression and position of the programmed double-strand breaks (DSBs) that initiate interhomologue recombination, essential to yield viable haploid gametes. We find that the level of H3K4me3 is constitutively higher close to DSB sites, independently of local gene expression levels. Without Set1, the H3K4 methylase, 84% of the DSB sites exhibit a severely reduced DSB frequency, the reduction being quantitatively correlated with the local level of H3K4me3 in wild-type cells. Further, we show that this differential histone mark is already established in vegetative cells, being higher in DSB-prone regions than in regions with no or little DSB. Taken together, our results demonstrate that H3K4me3 is a prominent and preexisting mark of active meiotic recombination initiation sites. Novel perspectives to dissect the various layers of the controls of meiotic DSB formation are discussed.

MeSH Terms
DNA Breaks, Double-Stranded DNA Repair DNA-Binding Proteins/genetics,physiology Gene Expression Regulation, Fungal Histone-Lysine N-Methyltransferase Histones/metabolism Lysine/metabolism Meiosis/physiology Methylation Recombination, Genetic Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins/genetics,physiology Transcription Factors/genetics,physiology
Chemicals
DNA-Binding Proteins Histones Saccharomyces cerevisiae Proteins Transcription Factors Histone-Lysine N-Methyltransferase SET1 protein, S cerevisiae Lysine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Borde Valérie
Institut Curie Centre de Recherche, UMR7147 CNRS, Université Pierre et Marie Curie, Paris, France.
Robine Nicolas
Lin Waka
Bonfils Sandrine
Géli Vincent
Nicolas Alain
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
1460-2075
Published
2009-01-21
Epub
2008-00-11
Pages
99-111
Language
English
Region
England
NLM ID
8208664
PMCID
PMC2634730
Subset
IM
Databases
GEO
Corrections
CommentIn
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