@article{61692fd6808445738339ff8a2de576ec,
title = "Dynamics of the Interaction of RecG Protein with Stalled Replication Forks",
abstract = "As a guardian of the bacterial genome, the RecG DNA helicase repairs DNA replication and rescues stalled replication. We applied atomic force microscopy (AFM) to directly visualize dynamics of RecG upon the interaction with replication fork substrates in the presence and absence of SSB using high-speed AFM. We directly visualized that RecG moves back and forth over dozens of base pairs in the presence of SSB. There is no RecG translocation in the absence of SSB. Computational modeling was performed to build models of Escherichia coli RecG in a free state and in complex with the fork. The simulations revealed the formation of complexes of RecG with the fork and identified conformational transitions that may be responsible for RecG remodeling that can facilitate RecG translocation along the DNA duplex. Such complexes do not form with the DNA duplex, which is in line with experimental data. Overall, our results provide mechanistic insights into the modes of interaction of RecG with the replication fork, suggesting a novel role of RecG in the repair of stalled DNA replication forks.",
author = "Zhiqiang Sun and Mohtadin Hashemi and Galina Warren and Bianco, {Piero R.} and Lyubchenko, {Yuri L.}",
note = "Funding Information: This work was supported by the National Institutes of Health (Grants R01 GM100156 to Y.L.L. and P.R.B. and R01 GM096039 and R01GM118006 to Y.L.L.) and the National Science Foundation (MCB 1515346). M.H. was partially supported by the Bukey Memorial Fellowship. Computational modeling was performed using computational facilities of the Holland Computing Center at the University of Nebraska (supported by the Nebraska Research Initiative) and the San Diego Supercomputing Center at the University of California at San Diego through the Extreme Science and Engineering Discovery Environment (XSEDE; supported by National Science Foundation Grant ACI-1053575 for XSEDE). . Computational modeling was performed using computational facilities of the Holland Computing Center at the University of Nebraska (supported by the Nebraska Research Initiative) and the San Diego Supercomputing Center at the University of California at San Diego through the Extreme Science and Engineering Discovery Environment (XSEDE; supported by National Science Foundation Grant ACI-1053575 for XSEDE). Funding Information: Computational modeling was performed using computational facilities of the Holland Computing Center at the University of Nebraska (supported by the Nebraska Research Initiative) and the San Diego Supercomputing Center at the University of California at San Diego through the Extreme Science and Engineering Discovery Environment (XSEDE; supported by National Science Foundation Grant ACI-1053575 for XSEDE). Funding Information: Mohtadin Hashemi: 0000-0003-2698-9761 Yuri L. Lyubchenko: 0000-0001-9721-8302 Author Contributions Y.L.L., Z.S., and M.H. conceived and designed the experiments. Z.S. and G.W. purified the DNA constructs and collected AFM images. P.R.B. provided all proteins. M.H. performed computational modeling. All authors wrote the manuscript. Funding This work was supported by the National Institutes of Health (Grants R01 GM100156 to Y.L.L. and P.R.B. and R01 GM096039 and R01GM118006 to Y.L.L.) and the National Science Foundation (MCB 1515346). M.H. was partially supported by the Bukey Memorial Fellowship. Notes The authors declare no competing financial interest. Publisher Copyright: {\textcopyright} 2018 American Chemical Society.",
year = "2018",
month = apr,
day = "3",
doi = "10.1021/acs.biochem.7b01235",
language = "English (US)",
volume = "57",
pages = "1967--1976",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "13",
}