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Structure and DNA bridging activity of the essential Rec114–Mei4 trimer interface

View ORCID ProfileKaixian Liu, View ORCID ProfileEmily M. Grasso, Stephen Pu, View ORCID ProfileShixin Liu, View ORCID ProfileDavid Eliezer, View ORCID ProfileScott Keeney
doi: https://doi.org/10.1101/2023.01.18.524603
Kaixian Liu
1Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, USA
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Emily M. Grasso
2Department of Biochemistry and Program in Structural Biology, Weill Cornell Medicine, New York, NY, USA
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Stephen Pu
1Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, USA
4Howard Hughes Medical Institute, Memorial Sloan Kettering Cancer Center, New York, USA
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Shixin Liu
3Laboratory of Nanoscale Biophysics and Biochemistry, The Rockefeller University, New York, NY, USA
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David Eliezer
2Department of Biochemistry and Program in Structural Biology, Weill Cornell Medicine, New York, NY, USA
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Scott Keeney
1Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, USA
4Howard Hughes Medical Institute, Memorial Sloan Kettering Cancer Center, New York, USA
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  • For correspondence: s-keeney@ski.mskcc.org
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Abstract

The DNA double-strand breaks (DSBs) that initiate meiotic recombination are formed by an evolutionarily conserved suite of factors that includes Rec114 and Mei4 (RM), which regulate DSB formation both spatially and temporally. In vivo, these proteins form large immunostaining foci that are integrated with higher order chromosome structures. In vitro, they form a 2:1 heterotrimeric complex that binds cooperatively to DNA to form large, dynamic condensates. However, understanding of the atomic structures and dynamic DNA binding properties of RM complexes is lacking. Here, we report a structural model of a heterotrimeric complex of the C-terminus of Rec114 with the N-terminus of Mei4, supported by nuclear magnetic resonance experiments. This minimal complex, which lacks the predicted intrinsically disordered region of Rec114, is sufficient to bind DNA and form condensates. Single-molecule experiments reveal that the minimal complex can bridge two or more DNA duplexes and can generate force to condense DNA through long-range interactions. AlphaFold2 predicts similar structural models for RM orthologs across diverse taxa despite their low degree of sequence similarity. These findings provide insight into the conserved networks of protein-protein and protein-DNA interactions that enable condensate formation and promote formation of meiotic DSBs.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted January 18, 2023.
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Structure and DNA bridging activity of the essential Rec114–Mei4 trimer interface
Kaixian Liu, Emily M. Grasso, Stephen Pu, Shixin Liu, David Eliezer, Scott Keeney
bioRxiv 2023.01.18.524603; doi: https://doi.org/10.1101/2023.01.18.524603
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Structure and DNA bridging activity of the essential Rec114–Mei4 trimer interface
Kaixian Liu, Emily M. Grasso, Stephen Pu, Shixin Liu, David Eliezer, Scott Keeney
bioRxiv 2023.01.18.524603; doi: https://doi.org/10.1101/2023.01.18.524603

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