#RAD51
‼️ Excited to share our new paper out now in @science.org ‼️

We describe a new tetrameric RAD51 paralog complex – XRCC3-RAD51C-RAD51D-XRCC2 – which caps the end of RAD51 filaments.

Link: www.science.org/doi/epdf/10....

Thread ⬇️ (1/8)
November 7, 2025 at 10:15 AM
How are Rad51 filaments formed during Homologous Recombination?

Jaigeeth Deveryshetty and Ayush Mistry describe the mechanism through the lens of Rad52, the yeast homolog of human BRCA2.

urldefense.com/v3/__https:/...
Mechanism of Rad51 filament formation by Rad52 and Rad55-Rad57 in homologous recombination
Nature Communications - The mediator protein Rad52 promotes Rad51 binding onto RPA-coated DNA to initiate homologous recombination. Here, the authors show that Rad52 sorts Rad51 into monomers and...
urldefense.com
July 21, 2025 at 12:34 PM
Excited to share our discovery of the RAD51 filament cap, built by a newly identified RAD51 paralog complex 🔬🧬
‼️ Excited to share our new paper out now in @science.org ‼️

We describe a new tetrameric RAD51 paralog complex – XRCC3-RAD51C-RAD51D-XRCC2 – which caps the end of RAD51 filaments.

Link: www.science.org/doi/epdf/10....

Thread ⬇️ (1/8)
November 7, 2025 at 10:22 AM
Excited to share our new pre-print. Direct, ensemble FRET assays developed by our lab reveal that assembly of Rad51 filaments at stalled replication sites via RPA/Rad51 exchange causes complete & irreversible PCNA unloading. Big implications for interplay between human DNA damage tolerance pathways
www.biorxiv.org
April 1, 2025 at 5:58 PM
Nice to be here! Take a look at our recent paper. Hope you like it: www.cell.com/molecular-ce...
RAD51 protects abasic sites to prevent replication fork breakage
Hanthi et al. found that RAD51 recognizes and binds to abasic sites. Together with BRCA2, RAD51 prevents the accumulation of abasic site-induced replicative DNA gaps (caused by DNA methylation, oxidat...
www.cell.com
November 12, 2024 at 10:37 AM
Want to know how homologous recombination defects are caused upon loss of BRCA2? Check out our recent efforts in uncovering this phenomenon just out in Science!
www.science.org/doi/10.1126/...
FIGNL1 inhibits homologous recombination in BRCA2 deficient cells by dissociating RAD51 filaments
Homologous recombination (HR) deficiency upon Breast Cancer Gene 2 (BRCA2) loss arises from defects in the formation of RAD51 nucleoprotein filaments. We demonstrate that loss of the anti-recombinase ...
www.science.org
October 30, 2025 at 9:52 PM
Excited to share my first co-first author paper! We uncovered a conserved role for RAD51/BRCA2 in protecting abasic sites at replication forks from MRE11 cleavage.
#ssDNA gaps, #DNMT1, #POLθ, #Cryo-EM of #RAD51 bound to AP sites, and much more! Check it out!
RAD51 protects abasic sites to prevent replication fork breakage
Hanthi et al. found that RAD51 recognizes and binds to abasic sites. Together with BRCA2, RAD51 prevents the accumulation of abasic site-induced replicative DNA gaps (caused by DNA methylation, oxidat...
www.cell.com
November 18, 2024 at 2:19 PM
Happy to share new work from my lab by co-authors Peng and Lee-when BRCA1 is absent, RAD51 is busy authors.elsevier.com/sd/article/S...
September 10, 2025 at 5:32 PM
Thrilled to share our new work on how the human RAD51 paralogs cooperate to build and stabilize RAD51 filaments, published today in Nature.

www.nature.com/articles/s41...

Congratulations to all authors!
BCDX2–CX3 and DX2–CX3 complexes assemble and stabilize RAD51 filaments - Nature
Nature - BCDX2–CX3 and DX2–CX3 complexes assemble and stabilize RAD51 filaments
www.nature.com
March 2, 2026 at 5:42 PM
RAD51 stabilizes neutrophil extracellular traps to compartmentalize inflammation | Science www.science.org/doi/10.1126/...
RAD51 stabilizes neutrophil extracellular traps to compartmentalize inflammation
Neutrophil extracellular traps (NETs) feature a branched chromatin architecture whose origin and function remain unknown. We found that NET branching is mediated by RAD51, a protein generating DNA jun...
www.science.org
August 21, 2026 at 6:19 AM
BRCA2 C-terminal clamp restructures RAD51 dimers to bind B-DNA for replication fork stability: Molecular Cell www.cell.com/molecular-ce...
BRCA2 C-terminal clamp restructures RAD51 dimers to bind B-DNA for replication fork stability
With detailed structural and molecular analyses, Longo et al. find that the BRCA2 C-terminal TR2, which is a critical cancer therapy resistance factor, reshapes the RAD51 dimer for B-DNA binding that ...
www.cell.com
June 5, 2025 at 7:52 PM
This ‘landmark’ study describes the structural mechanism of strand exchange by the RAD51 filament using cryogenic structural, biochemical, and single-molecule analyses.
buff.ly/Ieh84gj
August 26, 2025 at 10:02 AM
Among the anti-recombinases, FIGNL1 rules them all. So much that inactivating it brings BRCA2-deficient cells to life. Who is responsible for RAD51 loading without BRCA2/FIGNL1, check out the paper to find out! Great collaboration with @raychaudhurilab.bsky.social

www.science.org/doi/10.1126/...
October 30, 2025 at 8:41 PM
NEW in @science.org, so happy to contribute to our understanding of the molecular machine, Fidgetin-like 1 (FIGNL1), and elucidating the mechanism of why cells cannot survive when it is lost! #ScienceResearch science.org/doi/10.1126/... (1/7)
Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin
Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central player of several crucial processes in repairing DNA and protecting genome integrity, forms filamen...
science.org
December 5, 2024 at 7:32 PM
Over five years of work has gone into our new preprint! The #cryoEM structure of a human RAD51 filament caught at the point of strand exchange 🧬
www.biorxiv.org/content/10.1...
Structural mechanism of strand exchange by the RAD51 filament.
Homologous Recombination (HR) preserves genomic stability by repairing double-strand DNA breaks and ensuring efficient DNA replication. Central to HR is the strand-exchange reaction taking place within the three-stranded synapsis wherein a RAD51 nucleoprotein filament binds to a donor DNA. Here we present the cryoEM structure of a displacement loop of human RAD51 that captures the synaptic state when the filament has become tightly bound to the donor DNA. The structure elucidates the mechanism of strand exchange by RAD51, including the filament engagement with the donor DNA, the strand invasion and pairing with the complementary sequence of the donor DNA, the capture of the non-complementary strand and the polarity of the strand-exchange reaction. Our findings provide fundamental mechanistic insights into the biochemical reaction of eukaryotic HR. ### Competing Interest Statement The authors have declared no competing interest.
www.biorxiv.org
March 27, 2025 at 3:12 PM
December 5, 2024 at 9:11 PM
Really cool new cryoEM structure of RAD51 caught in the act of recombination initiation at a D-loop. elifesciences.org/reviewed-pre...
Structural mechanism of strand exchange by the RAD51 filament
elifesciences.org
June 15, 2025 at 9:37 PM
Pesquisa com camundongos revela que a falta da proteína RAD51 em óvulos provoca danos no genoma do embrião, reduz o número de filhotes e favorece o surgimento de alterações genéticas espontâneas. Achado abre caminho para novas abordagens em reprodução assistida. agencia.fapesp.br/59280
Falha no reparo do DNA materno compromete desenvolvimento embrionário e gera mutações pós-fecundação
Pesquisa com camundongos revela que a falta da proteína RAD51 em óvulos provoca danos no genoma do embrião, reduz o número de filhotes e favorece o surgimento de alterações genéticas espontâneas. Acha...
agencia.fapesp.br
September 28, 2026 at 12:02 PM
Happy to share our study by Francien Talens and many colleagues on RAD51 foci formation as a functional marker for PARPi sensitivity in ovarian cancer PDX models. academic.oup.com/narcancer/ar...
RAD51 recruitment but not replication fork stability associates with PARP inhibitor response in ovarian cancer patient-derived xenograft models
Abstract. Poly(ADP‐ribose) polymerase (PARP) inhibitors (PARPis) are currently used to treat BRCA1/2 mutant cancers. Although PARPi sensitivity has been at
academic.oup.com
November 30, 2024 at 8:56 AM
Nature research paper: BRCA2 prevents PARPi-mediated PARP1 retention to protect RAD51 filaments

https://go.nature.com/3QT0acq
BRCA2 prevents PARPi-mediated PARP1 retention to protect RAD51 filaments - Nature
The tumour-suppressor protein BRCA2 is discovered to have a previously undescribed role in maintaining genomic integrity and the sensitivity of PARP1 inhibitors.
go.nature.com
March 28, 2025 at 12:55 PM