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PRDM9 interactions with other proteins provide a link between recombination hotspots and the chromosomal axis in meiosis

ED. Parvanov, H. Tian, T. Billings, RL. Saxl, C. Spruce, R. Aithal, L. Krejci, K. Paigen, PM. Petkov,

. 2017 ; 28 (3) : 488-499. [pub] 20161208

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc17031235
E-zdroje Online Plný text

NLK Free Medical Journals od 1992 do Před 2 měsíci
PubMed Central od 1992 do Před 2 měsíci
Europe PubMed Central od 1992 do Před 2 měsíci
Open Access Digital Library od 1989-11-01
Open Access Digital Library od 1997-01-01

Odkazy

PubMed 27932493
DOI 10.1091/mbc.e16-09-0686
Knihovny.cz E-zdroje

In mammals, meiotic recombination occurs at 1- to 2-kb genomic regions termed hotspots, whose positions and activities are determined by PRDM9, a DNA-binding histone methyltransferase. We 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 coimmunoprecipitation from mouse spermatocytes, we identified four proteins that directly interact with PRDM9's KRAB domain, namely CXXC1, EWSR1, EHMT2, and CDYL. These proteins are coexpressed 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.

Citace poskytuje Crossref.org

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