Monomeric ZRANB3 drives replication fork reversal
4 affiliations
- 1Institute of Biochemical Sciences, National Taiwan University , Taipei 106 ,
- 2Department of Chemistry, National Taiwan University , Taipei 106 ,
- 3Institute of Biological Chemistry , Academia Sinica, Taipei 106 ,
- 4Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica , Taipei 106 ,
Abstract
Replication fork reversal is a central response to replication stress, yet how a SNF2 translocase coordinates the distinct mechanical steps required for this reaction remains elusive. Here, we define the mechanism by which ZRANB3 catalyzes fork reversal using biochemical, biophysical, and single-molecule approaches. ZRANB3 binds fork DNA as a monomer at the junction, establishing the minimal functional unit required for activity. Mechanistically, ZRANB3 combines ATP-dependent localized duplex opening with ATP-independent strand annealing to facilitate four-way junction formation, followed by directional branch migration that supports long-range fork reversal. Single-molecule fluorescence analyses further demonstrate that monomeric ZRANB3 is sufficient to drive fork reversal. Together, these findings define how ZRANB3 integrates distinct DNA remodeling activities within a single enzyme to catalyze fork reversal.
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BibTeX
@article{chen2026monomeric,
title = {{Monomeric ZRANB3 drives replication fork reversal}},
author = {Yen-Ju Chen and Yu-Hui Chiu and Chieh-Kai Liu and Hsuan Hsu and Kuan-Chi Wang and Guan-Ting Lian and Yi-An Chen and Sheng-Wei Lin and Hsin-Yung Yen and Hung-Wen Li and Peter Chi},
journal = {Nucleic Acids Research},
year = {2026},
month = oct,
doi = {10.1093/nar/gkag1034},
url = {https://academic.oup.com/nar/article/doi/10.1093/nar/gkag1034/9010722},
note = {CC BY},
}
RIS
TY - JOUR
TI - Monomeric ZRANB3 drives replication fork reversal
AU - Yen-Ju Chen
AU - Yu-Hui Chiu
AU - Chieh-Kai Liu
AU - Hsuan Hsu
AU - Kuan-Chi Wang
AU - Guan-Ting Lian
AU - Yi-An Chen
AU - Sheng-Wei Lin
AU - Hsin-Yung Yen
AU - Hung-Wen Li
AU - Peter Chi
PY - 2026
DA - 2026/10/01
JO - Nucleic Acids Research
DO - 10.1093/nar/gkag1034
UR - https://academic.oup.com/nar/article/doi/10.1093/nar/gkag1034/9010722
AB - Replication fork reversal is a central response to replication stress, yet how a SNF2 translocase coordinates the distinct mechanical steps required for this reaction remains elusive. Here, we define the mechanism by which ZRANB3 catalyzes fork reversal using biochemical, biophysical, and single-molecule approaches. ZRANB3 binds fork DNA as a monomer at the junction, establishing the minimal functional unit required for activity. Mechanistically, ZRANB3 combines ATP-dependent localized duplex opening with ATP-independent strand annealing to facilitate four-way junction formation, followed by directional branch migration that supports long-range fork reversal. Single-molecule fluorescence analyses further demonstrate that monomeric ZRANB3 is sufficient to drive fork reversal. Together, these findings define how ZRANB3 integrates distinct DNA remodeling activities within a single enzyme to catalyze fork reversal.
SN - 0305-1048
SN - 1362-4962
ER -