Isolation and Characterization of Monomeric Human RAD51: A Novel Tool for Investigating Homologous Recombination in Cancer
Abstract: DNA repair protein RAD51 is a key player in the homologous recombination pathway. Upon DNA damage, RAD51 is transported into the nucleus by BRCA2, where it can repair DNA double‐strand breaks. Due to the structural complexity and dynamics, researchers have not yet clarified the mechanistic details of every step of RAD51 recruitment and DNA repair. RAD51 possesses an intrinsic tendency to form oligomeric structures, which make it challenging to conduct biochemical and biophysical investigations. Here, for the first time, we report on the isolation and characterization of a human monomeric RAD51 recombinant form, obtained through a double mutation, which preserves the protein's integrity and functionality. We investigated different buffers to identify the most suitable condition needed to definitively stabilize the monomer. The monomer of human RAD51 provides the community with a unique biological tool for investigating RAD51‐mediated homologous recombination, and paves the way for more reliable structural, mechanistic, and drug discovery studies.
- Location
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                Deutsche Nationalbibliothek Frankfurt am Main
 
- Extent
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                Online-Ressource
 
- Language
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                Englisch
 
- Bibliographic citation
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                Isolation and Characterization of Monomeric Human RAD51: A Novel Tool for Investigating Homologous Recombination in Cancer ; day:20 ; month:11 ; year:2023 ; extent:14
 Angewandte Chemie / International edition. International edition ; (20.11.2023) (gesamt 14)
 
- Creator
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                Rinaldi, Francesco
 Schipani, Fabrizio
 Balboni, Beatrice
 Catalano, Federico
 Marotta, Roberto
 Myers, Samuel H.
 Previtali, Viola
 Veronesi, Marina
 Scietti, Luigi
 Cecatiello, Valentina
 Pasqualato, Sebastiano
 Ortega, Jose Antonio
 Girotto, Stefania
 Cavalli, Andrea
 
- DOI
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                        10.1002/anie.202312517
- URN
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                        urn:nbn:de:101:1-2023112114093444263633
- Rights
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                        Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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                        15.08.2025, 7:29 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Rinaldi, Francesco
- Schipani, Fabrizio
- Balboni, Beatrice
- Catalano, Federico
- Marotta, Roberto
- Myers, Samuel H.
- Previtali, Viola
- Veronesi, Marina
- Scietti, Luigi
- Cecatiello, Valentina
- Pasqualato, Sebastiano
- Ortega, Jose Antonio
- Girotto, Stefania
- Cavalli, Andrea
