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

Details

Serval ID
serval:BIB_C987AB7FF934
Type
Article: article from journal or magazin.
Collection
Publications
Title
Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.
Journal
Nucleic Acids Research
Author(s)
Kang H.A., Shin H.C., Kalantzi A.S., Toseland C.P., Kim H.M., Gruber S., Peraro M.D., Oh B.H.
ISSN
1362-4962 (Electronic)
ISSN-L
0305-1048
Publication state
Published
Issued date
2015
Peer-reviewed
Oui
Volume
43
Number
7
Pages
3841-3856
Language
english
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 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.
Keywords
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
Pubmed
Web of science
Open Access
Yes
Create date
17/08/2016 9:56
Last modification date
20/08/2019 15:44
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