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. 2015 Mar 27;43(8):4055–4066. doi: 10.1093/nar/gkv259

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 8. — Model for the mechanism of the Hop2-Mnd1-RAD51/DMC1-ssDNA ensemble. (a) Cartoon showing the Hop2-Mnd1 complex and functional domains in the protein subunits. (b) Our model posits that Hop2–Mnd1 associates with RAD51/DMC1 through an interface contributed by the C-termini of Hop2 and Mnd1, stabilizes the RAD51/DMC1 presynaptic filament via its ssDNA-binding activity within the C-terminus of Hop2 and helps capture duplex DNA by its dsDNA binding functions located in the N-termini of Hop2 and Mnd1. These attributes of Hop2-Mnd1 enhance the efficiency at which a duplex DNA molecule is engaged and sampled for homology by the RAD51/DMC1 presynaptic filament.