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

Détails

ID Serval
serval:BIB_C987AB7FF934
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.
Périodique
Nucleic Acids Research
Auteur⸱e⸱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
Statut éditorial
Publié
Date de publication
2015
Peer-reviewed
Oui
Volume
43
Numéro
7
Pages
3841-3856
Langue
anglais
Résumé
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.
Mots-clé
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
Oui
Création de la notice
17/08/2016 9:56
Dernière modification de la notice
20/08/2019 15:44
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