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

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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 alpha-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.
Publisher
OXFORD UNIV PRESS
Issue Date
2015-04
Language
English
Article Type
Article
Keywords

DOUBLE-STRAND BREAKS; NUCLEIC-ACID STRUCTURES; PROTEIN COMPLEX; FISSION YEAST; SACCHAROMYCES-CEREVISIAE; RAD51 RECOMBINASE; DNA RECOMBINATION; HOP2 PROTEIN; MEIOSIS; DMC1

Citation

NUCLEIC ACIDS RESEARCH, v.43, no.7, pp.3841 - 3856

ISSN
0305-1048
DOI
10.1093/nar/gkv172
URI
http://hdl.handle.net/10203/199068
Appears in Collection
BS-Journal Papers(저널논문)
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