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Structure paper

TitleRAD51AP1 is a versatile RAD51 modulator.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 49, Page e2514728122, Year 2025
Publish dateDec 9, 2025
AuthorsLucas Kuhlen / Bilge Argunhan / Pengtao Liang / Janet Zhong / Laura Masino / Xiaodong Zhang /
PubMed AbstractRAD51AP1 is an emergent key factor in homologous recombination (HR), the major pathway for accurate repair of DNA double-strand breaks, and in alternative lengthening of telomeres (ALT). Depletion of ...RAD51AP1 is an emergent key factor in homologous recombination (HR), the major pathway for accurate repair of DNA double-strand breaks, and in alternative lengthening of telomeres (ALT). Depletion of RAD51AP1 diminishes HR and overexpression is common in cancer, where it is associated with malignancy. Here, we show that RAD51AP1 has a hitherto unknown role in modulating the RAD51 recombinase, the central player in HR. Through a combination of biochemistry and structural biology, we reveal that RAD51AP1 possesses at least three RAD51-binding sites that facilitate its binding across two adjacent RAD51 molecules. We uncover a previously unidentified RAD51-binding mode that stabilizes the RAD51 N-terminal domain and protomer interface in the filaments. We uncover a previously undescribed role for RAD51AP1 in stabilizing RAD51-ssDNA filaments and promoting strand exchange. Our structural data provide the molecular basis for how RAD51AP1 binding induces conformational changes that promote RAD51 DNA association and oligomerization, therefore promoting filament nucleation, stabilization, and strand exchange. Further, we resolved structures of RAD51-ssDNA filaments in the presence of Mg-ATP and upon hydrolysis to Mg-ADP, revealing that RAD51 filaments expand upon ATP hydrolysis and explaining how ADP reduces RAD51-DNA binding. Our findings reveal RAD51AP1 as a versatile RAD51 modulator and RAD51 filament remodeler and shed previously unidentified insights into the modulation of HR, which is critical for the maintenance of genome stability.
External linksProc Natl Acad Sci U S A / PubMed:41337480 / PubMed Central
MethodsEM (single particle) / EM (helical sym.)
Resolution2.98 - 3.63 Å
Structure data

53239

9qn8

EMDB-53239, PDB-9qn8:
RAD51 filament in complex with calcium and ATP bound by the RAD51AP1 C-terminus
Method: EM (single particle) / Resolution: 3.14 Å

53241

9qna

EMDB-53241, PDB-9qna:
RAD51 filament in complex with magnesium and ATP
Method: EM (helical sym.) / Resolution: 3.26 Å

53242

9qnb

EMDB-53242, PDB-9qnb:
RAD51 filament in complex with magnesium and ADP
Method: EM (helical sym.) / Resolution: 3.63 Å

53243

9qnc

EMDB-53243, PDB-9qnc:
RAD51 filament in complex with magnesium and ATP bound by the RAD51AP1 C-terminus
Method: EM (single particle) / Resolution: 2.98 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-CA:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / RAD51 recombinase / RAD51AP1 / filament modulation / homologous recombination / nucleotide hydrolysis

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