Article: article from journal or magazin.
Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.
Nucleic Acids Research
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 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.
Amino Acid Sequence, Animals, Base Sequence, Chromosomal Proteins, Non-Histone/chemistry, Chromosomal Proteins, Non-Histone/physiology, Crystallography, X-Ray, DNA Primers, Humans, Meiosis/physiology, Molecular Dynamics Simulation, Molecular Sequence Data, Protein Conformation, Recombination, Genetic, Saccharomyces cerevisiae Proteins/chemistry, Saccharomyces cerevisiae Proteins/physiology, Sequence Homology, Amino Acid
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