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Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.


ABSTRACT: In meiotic DNA recombination, the Hop2-Mnd1 complex promotes Dmc1-mediated single-stranded DNA (ssDNA) invasion into homologous chromosomes to form a synaptic complex by a yet-unclear mechanism. Here, the crystal structure of Hop2-Mnd1 reveals that it forms a curved rod-like structure consisting of three leucine zippers and two kinked junctions. One end of the rod is linked to two juxtaposed winged-helix domains, and the other end is capped by extra ?-helices to form a helical bundle-like structure. Deletion analysis shows that the helical bundle-like structure is sufficient for interacting with the Dmc1-ssDNA nucleofilament, and molecular modeling suggests that the curved rod could be accommodated into the helical groove of the nucleofilament. Remarkably, the winged-helix domains are juxtaposed at fixed relative orientation, and their binding to DNA is likely to perturb the base pairing according to molecular simulations. These findings allow us to propose a model explaining how Hop2-Mnd1 juxtaposes Dmc1-bound ssDNA with distorted recipient double-stranded DNA and thus facilitates strand invasion.

SUBMITTER: Kang HA 

PROVIDER: S-EPMC4402518 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature

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Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.

Kang Hyun-Ah HA   Shin Ho-Chul HC   Kalantzi Alexandra-Styliani AS   Toseland Christopher P CP   Kim Hyun-Min HM   Gruber Stephan S   Peraro Matteo Dal MD   Oh Byung-Ha BH  

Nucleic acids research 20150303 7


In meiotic DNA recombination, the Hop2-Mnd1 complex promotes Dmc1-mediated single-stranded DNA (ssDNA) invasion into homologous chromosomes to form a synaptic complex by a yet-unclear mechanism. Here, the crystal structure of Hop2-Mnd1 reveals that it forms a curved rod-like structure consisting of three leucine zippers and two kinked junctions. One end of the rod is linked to two juxtaposed winged-helix domains, and the other end is capped by extra α-helices to form a helical bundle-like struct  ...[more]

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