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Identification of PRDM9 partners

ABSTRACT: PRDM9 specifies the sites of meiotic DNA double strand break that initiate meiotic recombination in mice and humans. PRDM9 is known to bind to specific DNA sequences with its DNA binding domain, to induce H3K4me3 and H3K36me3 to adjacent nucleosomes through its methyltransferase activity, and to recruit or activate the meiotic DSB machinery. To understand how PRDM9 executes these various steps, we set up to identify its partners. This was performed by a proteomic approach where protein extracts from mouse testis were immunoprecipitated with anti-PRDM9 antibody for mass spectrometry analysis.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Testis

SUBMITTER: Oana Vigy

LAB HEAD: Bernard de Massy

PROVIDER: PXD017337 | Pride | 2020-12-03

REPOSITORIES: Pride

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

Imai Yukiko Y Biot Mathilde M Clément Julie Aj JA Teragaki Mariko M Urbach Serge S Robert Thomas T Baudat Frédéric F Grey Corinne C de Massy Bernard B

eLife 20201013

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 sit ...[more]

PMID: 33047671

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