The YoaA-χ helicase modulates the dynamics of single-stranded DNA binding protein on DNA

Savannah J. Weeks-Pollenz, Matthew J. Petrides, Kaylie A. Padgett-Pagliai, Robert Davis, Kathryn K. Harris and Linda B. Bloom ()
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Savannah J. Weeks-Pollenz: University of Florida
Matthew J. Petrides: University of Florida
Kaylie A. Padgett-Pagliai: University of Florida
Robert Davis: University of Florida
Kathryn K. Harris: University of Florida
Linda B. Bloom: University of Florida

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract The Escherichia coli helicase, YoaA, and DNA polymerase III subunit, χ, form a complex (YoaA-χ) that promotes tolerance to the DNA chain-terminator 3ˈ-azidothymidine (AZT). Single-stranded DNA binding protein (SSB), which accumulates at stalled replication forks, also contributes to AZT tolerance through interactions with χ. Here we show that in vitro, χ mediates interactions between YoaA and SSB that modulate helicase activity in a substrate-specific manner with little effect on overhang DNA but inhibiting unwinding of forked DNA. SSB similarly affects the activity of the YoaA paralog, DinG. Single-molecule experiments show that SSB translocates with YoaA-χ, increasing both the lifetime and frequency of SSB binding events. Mutational analyses show that χ binds at the back of YoaA relative to the direction of translocation supporting a model in which YoaA-χ pulls SSB along DNA as it translocates. To our knowledge, this is the first demonstration of a mechanoenzyme pulling SSB along ssDNA.

Date: 2025
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DOI: 10.1038/s41467-025-60215-4

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