Online today @science.org 👀Molecular basis of FIGNL1 in dissociating RAD51 from #DNA and #chromatin by @alexcarver.bsky.social @layates.bsky.social et al. in @imperialcollegeldn.bsky.social @mskcancercenter.bsky.social
www.science.org/doi/10.1126/...

Shout out too to all the authors and facilities:
@layates.bsky.social
@imperialcollegeldn.bsky.social
@mskcancercenter.bsky.social
(and those not on BlueSky!)
Thank you to @stephcrystallab.bsky.social
for the lovely rendering of the FIGNL1 hexamer (7/7)

This work would not be possible without the cross-Atlantic collaboration between scientists in both London and New York City, and the guidance and tutelage of two giants in the DNA repair field, Professors Xiaodong Zhang and Maria Jasin (6/7)

Our study has answered how inactivation of FIGNL1 results in cell death and provides the first molecular evidence for a unique mechanism of RAD51 removal from DNA (5/7)

We validated the model in vivo, showed that inactivating FIGNL1 resulted in RAD51 binding to DNA even in the absence of DNA damage, and mutating key regions seen in the structure caused cell death (4/7)

Using biochemical and structural approaches, we show that FIGNL1 forms a ring around RAD51 and removes it from DNA. Mutating key regions of the FIGNL1 ring resulted in loss of RAD51 removal (3/7)

FIGNL1 has been shown to be essential for survival, and previous studies have shown FIGNL1 acts as a supervisor for the DNA repair protein, RAD51; however, the exact mechanism of both is unclear (2/7)

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)

Congratulations Alessandro, so nice to see this out!