%0 Journal Article %A Emil D. Parvanov %A Hui Tian %A Timothy Billings %A Ruth L. Saxl %A Catrina Spruce %A Rakesh Aithal %A Lumir Krejci %A Kenneth Paigen %A Petko M. Petkov %T PRDM9 forms a multiprotein complex tethering recombination hotspots to the chromosomal axis %D 2016 %R 10.1101/056713 %J bioRxiv %P 056713 %X In mammals, meiotic recombination occurs at 1-2 kb genomic regions termed hotspots, whose positions and activities are determined by PRDM9, a DNA-binding histone methyltransferase. We now show that the KRAB domain of PRDM9 forms complexes with additional proteins to allow hotspots to proceed into the next phase of recombination. By a combination of yeast-two hybrid assay, in vitro binding, and co-immunoprecipitation from mouse spermatocytes, we identified four proteins that directly interact with PRDM9’s KRAB domain, namely CXXC1, EWSR1, EHMT2, and CDYL. These proteins are co-expressed in spermatocytes at the early stages of meiotic prophase I, the limited period when PRDM9 is expressed. We also detected association of PRDM9-bound complexes with the meiotic cohesin REC8 and the synaptonemal complex proteins SYCP3 and SYCP1. Our results suggest a model in which PRDM9-bound hotspot DNA is brought to the chromosomal axis by the action of these proteins, ensuring the proper chromatin and spatial environment for subsequent recombination events. %U https://www.biorxiv.org/content/biorxiv/early/2016/09/16/056713.full.pdf