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Mer2 binds directly to nucleosomes and axial proteins as the keystone of meiotic recombination

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Rousova,  D       
Weir Group, Friedrich Miescher Laboratory, Max Planck Society;

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Funk,  S       
Weir Group, Friedrich Miescher Laboratory, Max Planck Society;

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Weir,  JR       
Weir Group, Friedrich Miescher Laboratory, Max Planck Society;

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Citation

Rousova, D., Funk, S., & Weir, J. (2020). Mer2 binds directly to nucleosomes and axial proteins as the keystone of meiotic recombination. Poster presented at Cell Bio 2020 Virtual: An Online ASCB|EMBO Meeting.


Cite as: https://hdl.handle.net/21.11116/0000-000D-1E9C-3
Abstract
One of the defining features of sexual reproduction is the recombination events that take place during meiosis I. Recombination is both evolutionarily advantageous, but also mechanistically necessary to form the crossovers that link homologous chromosomes. Meiotic recombination is initiated through the placement of programmed double‐strand DNA breaks (DSBs) mediated by the protein Spo11. The timing, number, and physical placement of DSBs are carefully controlled through a variety of protein machinery. Previous work has implicated Mer2(IHO1 in mammals) to be involved in both the placement of breaks, and their timing. In this study we use a combination of protein biochemistry and biophysics to extensively characterise various roles of the Mer2. We gain further insights into the details of Mer2 interaction with the PHD protein Spp1, reveal that Mer2 is a novel nucleosome binder, and suggest how Mer2’s interaction with the axial HORMA domain protein Hop1 (HORMAD1/2 in mammals) is controlled.