Crosstalk between CST and RPA regulates RAD51 activity during replication stress

Kai-Hang Lei, Han-Lin Yang, Hao-Yen Chang, Hsin-Yi Yeh, Dinh Duc Nguyen, Tzu-Yu Lee, Xinxing Lyu, Megan Chastain, Weihang Chai, Hung-Wen Li () and Peter Chi ()
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Kai-Hang Lei: National Taiwan University
Han-Lin Yang: National Taiwan University
Hao-Yen Chang: National Taiwan University
Hsin-Yi Yeh: National Taiwan University
Dinh Duc Nguyen: Loyola University Chicago Stritch School of Medicine
Tzu-Yu Lee: National Taiwan University
Xinxing Lyu: Loyola University Chicago Stritch School of Medicine
Megan Chastain: Washington State University
Weihang Chai: Loyola University Chicago Stritch School of Medicine
Hung-Wen Li: National Taiwan University
Peter Chi: National Taiwan University

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: Abstract Replication stress causes replication fork stalling, resulting in an accumulation of single-stranded DNA (ssDNA). Replication protein A (RPA) and CTC1-STN1-TEN1 (CST) complex bind ssDNA and are found at stalled forks, where they regulate RAD51 recruitment and foci formation in vivo. Here, we investigate crosstalk between RPA, CST, and RAD51. We show that CST and RPA localize in close proximity in cells. Although CST stably binds to ssDNA with a high affinity at low ionic strength, the interaction becomes more dynamic and enables facilitated dissociation at high ionic strength. CST can coexist with RPA on the same ssDNA and target RAD51 to RPA-coated ssDNA. Notably, whereas RPA-coated ssDNA inhibits RAD51 activity, RAD51 can assemble a functional filament and exhibit strand-exchange activity on CST-coated ssDNA at high ionic strength. Our findings provide mechanistic insights into how CST targets and tethers RAD51 to RPA-coated ssDNA in response to replication stress.

Date: 2021
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DOI: 10.1038/s41467-021-26624-x

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