PRDM9 activity depends on HELLS and promotes local 5-hydroxymethylcytosine enrichment.


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
13 10 2020
Historique:
received: 20 03 2020
accepted: 16 09 2020
pubmed: 14 10 2020
medline: 15 5 2021
entrez: 13 10 2020
Statut: epublish

Résumé

Meiotic recombination starts with the formation of DNA double-strand breaks (DSBs) at specific genomic locations that correspond to PRDM9-binding sites. The molecular steps occurring from PRDM9 binding to DSB formation are unknown. Using proteomic approaches to find PRDM9 partners, we identified HELLS, a member of the SNF2-like family of chromatin remodelers. Upon functional analyses during mouse male meiosis, we demonstrated that HELLS is required for PRDM9 binding and DSB activity at PRDM9 sites. However, HELLS is not required for DSB activity at PRDM9-independent sites. HELLS is also essential for 5-hydroxymethylcytosine (5hmC) enrichment at PRDM9 sites. Analyses of 5hmC in mice deficient for SPO11, which catalyzes DSB formation, and in PRDM9 methyltransferase deficient mice reveal that 5hmC is triggered at DSB-prone sites upon PRDM9 binding and histone modification, but independent of DSB activity. These findings highlight the complex regulation of the chromatin and epigenetic environments at PRDM9-specified hotspots.

Identifiants

pubmed: 33047671
doi: 10.7554/eLife.57117
pii: 57117
pmc: PMC7599071
doi:
pii:

Substances chimiques

5-hydroxymethylcytosine 1123-95-1
5-Methylcytosine 6R795CQT4H
Histone-Lysine N-Methyltransferase EC 2.1.1.43
PRDM9 protein, human EC 2.1.1.43
prdm9 protein, mouse EC 2.1.1.43
Endodeoxyribonucleases EC 3.1.-
meiotic recombination protein SPO11 EC 3.1.-
DNA Helicases EC 3.6.4.-
HELLS protein, human EC 5.99.-
Hells protein, mouse EC 5.99.-

Banques de données

GEO
['GSE145768']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : ERC
ID : 322788
Pays : International
Organisme : MSDAVenir
ID : Gene-IGH
Pays : International
Organisme : European Research Council
ID : 322788
Pays : International

Informations de copyright

© 2020, Imai et al.

Déclaration de conflit d'intérêts

YI, MB, JC, MT, SU, TR, FB, CG No competing interests declared, Bd Reviewing editor, eLife

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Auteurs

Yukiko Imai (Y)

Institut de Génétique Humaine (IGH), Centre National de la Recherche Scientifique, Univ Montpellier, Montpellier, France.

Mathilde Biot (M)

Institut de Génétique Humaine (IGH), Centre National de la Recherche Scientifique, Univ Montpellier, Montpellier, France.

Julie Aj Clément (JA)

Institut de Génétique Humaine (IGH), Centre National de la Recherche Scientifique, Univ Montpellier, Montpellier, France.

Mariko Teragaki (M)

Institut de Génétique Humaine (IGH), Centre National de la Recherche Scientifique, Univ Montpellier, Montpellier, France.

Serge Urbach (S)

Institut de Génomique Fonctionnelle, Université de Montpellier, CNRS, INSERM, Montpellier, France.

Thomas Robert (T)

Institut de Génétique Humaine (IGH), Centre National de la Recherche Scientifique, Univ Montpellier, Montpellier, France.

Frédéric Baudat (F)

Institut de Génétique Humaine (IGH), Centre National de la Recherche Scientifique, Univ Montpellier, Montpellier, France.

Corinne Grey (C)

Institut de Génétique Humaine (IGH), Centre National de la Recherche Scientifique, Univ Montpellier, Montpellier, France.

Bernard de Massy (B)

Institut de Génétique Humaine (IGH), Centre National de la Recherche Scientifique, Univ Montpellier, Montpellier, France.

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