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Authors
Hohl, Marcel
Yu, You
Kuryavyi, Vitaly https://orcid.org/0000-0003-3938-6652
Patel, Dinshaw J. https://orcid.org/0000-0002-9779-7778
Petrini, John https://orcid.org/0000-0001-5102-5679
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Funding
Funding for this research was provided by:
U.S. Department of Health & Human Services | National Institutes of Health (R35 GM136278-04)
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Article History
Received: 16 November 2024
Accepted: 19 July 2025
First Online: 12 August 2025
Competing interests
: The authors declare no competing interests.
: In vivo, the S. cerevisiae Mre11 complex consists of Mre11, Rad50 and Xrs2. We were unable to obtain particles of MRX for our studies. This restricted our structure guided genetic analyses to Mre11 and Rad50. Also, we only got particles for MREQ and not for MRWT, thus preventing us from getting structural insights of the complex after ATP-hydrolysis. In addition, the flexibility of the extended Rad50 coiled coil domain precluded us from obtaining structural information regarding suppressor mutations that reside within the coils, thus limiting our ability to determine the mechanism(s) of suppression. The molecular defect of rad50-3KA was mostly informed from Molecular Dynamics simulations and future studies are required to test the suggested model.
