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
Institution
Title
Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.
Journal
Nucleic Acids Research
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