ArticleThe Journal of biological chemistry2014
Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Mortalin and PINK1/Parkin-Mediated Mitophagy Represent Ovarian Cancer-Selective Targets for Drug Development.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The Hop2-Mnd1 Complex and Its Regulation of Homologous Recombination.Biomolecules · 2023Review
- The Arabidopsis HOP2 gene has a role in preventing illegitimate connections between nonhomologous chromosome regions.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2022Article
- Dynamic interactions of the homologous pairing 2 (Hop2)-meiotic nuclear divisions 1 (Mnd1) protein complex with meiotic presynaptic filaments in budding yeast.The Journal of biological chemistry · 2019Article
- Biochemical attributes of mitotic and meiotic presynaptic complexes.DNA repair · 2018Review
- Tolerance of DNA Mismatches in Dmc1 Recombinase-mediated DNA Strand Exchange.The Journal of biological chemistry · 2016Article
- Comprehensive Cross-Linking Mass Spectrometry Reveals Parallel Orientation and Flexible Conformations of Plant HOP2-MND1.Journal of proteome research · 2015Article
- Connecting by breaking and repairing: mechanisms of DNA strand exchange in meiotic recombination.The FEBS journal · 2015Review
- Significance of ligand interactions involving Hop2-Mnd1 and the RAD51 and DMC1 recombinases in homologous DNA repair and XX ovarian dysgenesis.Nucleic acids research · 2015Article
- Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.Nucleic acids research · 2015Article
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
Abstract
The HOP2 protein is required for efficient double-strand break repair which ensures the proper synapsis of homologous chromosomes and normal meiotic progression. We previously showed that in vitro HOP2 shows two distinctive activities: when it is incorporated into a HOP2-MND1 heterodimer, it stimulates DMC1 and RAD51 recombination activities, and the purified HOP2 alone is proficient in promoting strand invasion. The structural and biochemical basis of HOP2 action in recombination are poorly understood; therefore, they are the focus of this work. Herein, we present the solution structure of the amino-terminal portion of mouse HOP2, which contains a typical winged helix DNA-binding domain. Together with NMR spectral changes in the presence of double-stranded DNA, protein docking on DNA, and mutation analysis to identify the amino acids involved in DNA coordination, our results on the three-dimensional structure of HOP2 provide key information on the fundamental structural and biochemical requirements directing the interaction of HOP2 with DNA. These results, in combination with mutational experiments showing the role of a coiled-coil structural feature involved in HOP2 self-association, allow us to explain important aspects of the function of HOP2 in recombination.
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