In this section
@article{Liang:2026:10.1038/s41467-026-78608-4,
author = {Liang, P and Tye, S and Ertl, da Costa J and Maharshi, N and Argunhan, B and Kuhlen, L and Battley, M and McCormack, EA and Heyer, W-D and Lobrich, M and Zhang, X},
doi = {10.1038/s41467-026-78608-4},
journal = {Nature Communications},
title = {Structures and molecular mechanisms of RAD54B in modulating homologous recombination},
url = {http://dx.doi.org/10.1038/s41467-026-78608-4},
year = {2026}
}
TY - JOUR
AB - Genome stability is essential for cellular viability yet constantly threatened by DNA-damaging agents. Among these, DNA double-strand breaks (DSBs) are particularly harmful and in S/G2 phases are faithfully repaired through homologous recombination (HR). The RAD51 recombinase forms nucleoprotein filaments on single-stranded DNA (ssDNA) that performs critical functions in HR. The efficiency of HR depends on precise regulation of RAD51 filament dynamics by accessory factors, including RAD54B, a double-strand DNA-dependent ATPase. Here, using cryogenic electron microscopy, mutagenesis, and biochemical assays, we show that RAD54B stabilizes RAD51–DNA filaments, inhibits RAD51 ATPase activity, and promotes D-loop formation and strand exchange. RAD54B contains two main RAD51-interacting sites and a β-domain that bridges RAD51 protomers, is positioned to contact donor dsDNA, and regulates RAD54B’s ATPase activity. Cellular assays reveal that the RAD51-interacting sites are required for repairing DSBs by HR in human cells. Our findings uncover a modular architecture and mechanistic framework for RAD54B’s critical role in genome maintenance.
AU - Liang,P
AU - Tye,S
AU - Ertl,da Costa J
AU - Maharshi,N
AU - Argunhan,B
AU - Kuhlen,L
AU - Battley,M
AU - McCormack,EA
AU - Heyer,W-D
AU - Lobrich,M
AU - Zhang,X
DO - 10.1038/s41467-026-78608-4
PY - 2026///
SN - 2041-1723
TI - Structures and molecular mechanisms of RAD54B in modulating homologous recombination
T2 - Nature Communications
UR - http://dx.doi.org/10.1038/s41467-026-78608-4
ER -