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TitleStructural insight into how RAD51 paralog exchange regulates RAD51 filament formation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 33, Issue 5, Page 768-781, Year 2026
Publish dateApr 22, 2026
AuthorsYashpal Rawal / Youngho Kwon / Lijia Jia / Eliza A Ruben / Jae-Hoon Ji / Lijuan Guo / Caleb M Stratton / Digant Nayak / Miriam Tovar / Qingming Fang / Mohd Azrin Jamalruddin / Shuo Zhou / Sahiti Kuppa / Shahrez Syed / Angela M Jasper / Jeffrey N Katz / Cody M Rogers / Hardeep Kaur / Lorena Samentar / Weixing Zhao / Eloise Dray / Fang Zhang / Svetla Stoilova-McPhie / Alexander B Taylor / Sandeep Burma / Manjeet K Rao / David S Libich / Robert Hromas / Alexander V Mazin / Maria Jasin / Daohong Zhou / Kara A Bernstein / Eric C Greene / Elizabeth V Wasmuth / Patrick Sung / Shaun K Olsen /
PubMed AbstractHomologous recombination (HR) repairs DNA double-strand breaks and stabilizes stressed replication forks, and HR deficiency promotes genome instability and cancer. HR requires assembly of RAD51 ...Homologous recombination (HR) repairs DNA double-strand breaks and stabilizes stressed replication forks, and HR deficiency promotes genome instability and cancer. HR requires assembly of RAD51 nucleoprotein filaments on single-stranded DNA (ssDNA), a process regulated by the human RAD51 paralogs RAD51C, XRCC3, RAD51D and XRCC2. Here, using cryo-electron microscopy, we find that the RAD51-XRCC3-RAD51C complex (RAD51-X3C) assembles into an octamer in which XRCC3 engages the RAD51 DNA-binding surface and RAD51 subunits adopt a misaligned configuration incompatible with filament formation. These features define an autoinhibited RAD51-X3C state that limits nonproductive RAD51 binding to double-stranded DNA or RNA-DNA hybrids while preserving RAD51 availability for ssDNA-dependent strand exchange. We further show that the RAD51D-XRCC2 paralog complex remodels RAD51-X3C into a pentameric RAD51-X3CDX2 assembly by engaging the exposed RAD51C surface and disrupting contacts that stabilize the octamer. This remodeling exposes the RAD51 DNA-binding interface, enhances RAD51-ssDNA filament assembly, and promotes strand exchange on RPA-coated ssDNA, and yields a filament-compatible paralog assembly that integrates into ssDNA-bound RAD51 filaments. Together, these findings establish paralog exchange as a mechanism that converts an autoinhibited RAD51-X3C octamer into an activated RAD51-X3CDX2 pentamer to regulate RAD51 filament formation during HR and replication fork preservation.
External linksNat Struct Mol Biol / PubMed:42020761 / PubMed Central
MethodsEM (single particle)
Resolution2.95 - 3.51 Å
Structure data

70624

9omy

EMDB-70624, PDB-9omy:
Cryo-EM structure of an octameric RAD51-XRCC3-RAD51C (RAD51-X3C) complex
Method: EM (single particle) / Resolution: 3.25 Å

70625

9omz

EMDB-70625, PDB-9omz:
Cryo-EM structure of a pentameric RAD51-XRCC3-RAD51C-RAD51D-XRCC2 (51-X3CDX2) complex.
Method: EM (single particle) / Resolution: 3.51 Å

70627

9on2

EMDB-70627, PDB-9on2:
Cryo-EM structure of a tetrameric XRCC3-RAD51C-RAD51D-XRCC2 complex
Method: EM (single particle) / Resolution: 3.16 Å

75014

9zzr

EMDB-75014, PDB-9zzr:
Cryo-EM Structure of a RAD51 filament bound by ssDNA and the XRCC3-RAD51C-RAD51D-XRCC2 paralog complex
Method: EM (single particle) / Resolution: 2.95 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / Octamer / RAD51 / XRCC3 / RAD51C / Pentameric / RAD51D / XRCC2 / Tetrameric / DNA BINDING PROTEIN/DNA / DNA BINDING PROTEIN-DNA complex

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