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Title | Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 6215, Year 2023 |
Publish date | Oct 5, 2023 |
Authors | Jaigeeth Deveryshetty / Rahul Chadda / Jenna R Mattice / Simrithaa Karunakaran / Michael J Rau / Katherine Basore / Nilisha Pokhrel / Noah Englander / James A J Fitzpatrick / Brian Bothner / Edwin Antony / |
PubMed Abstract | Homologous recombination (HR) is an essential double-stranded DNA break repair pathway. In HR, Rad52 facilitates the formation of Rad51 nucleoprotein filaments on RPA-coated ssDNA. Here, we decipher ...Homologous recombination (HR) is an essential double-stranded DNA break repair pathway. In HR, Rad52 facilitates the formation of Rad51 nucleoprotein filaments on RPA-coated ssDNA. Here, we decipher how Rad52 functions using single-particle cryo-electron microscopy and biophysical approaches. We report that Rad52 is a homodecameric ring and each subunit possesses an ordered N-terminal and disordered C-terminal half. An intrinsic structural asymmetry is observed where a few of the C-terminal halves interact with the ordered ring. We describe two conserved charged patches in the C-terminal half that harbor Rad51 and RPA interacting motifs. Interactions between these patches regulate ssDNA binding. Surprisingly, Rad51 interacts with Rad52 at two different bindings sites: one within the positive patch in the disordered C-terminus and the other in the ordered ring. We propose that these features drive Rad51 nucleation onto a single position on the DNA to promote formation of uniform pre-synaptic Rad51 filaments in HR. |
External links | Nat Commun / PubMed:37798272 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.5 Å |
Structure data | EMDB-29695, PDB-8g3g: |
Source |
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Keywords | RECOMBINATION / Recombination mediator protein / DNA repair / Apo structure / Decamer |