Jennifer A. Surtees

University at Buffalo, State University of New York

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Ilya J. Finkelstein

The University of Texas at Austin

Gregory M. Williams

University at Buffalo, State University of New York

Fuyang Li

Shuguang Hospital

Ja-Hwan Seol

The University of Texas Health Science Center at San Antonio

Yoori Kim

Seoul National University

Iluminada Gallardo

University of Florida

John D. Huck

Yale University

Xiaolei Li

First Affiliated Hospital of Jiangxi Medical College

Maxwell W. Brown

The University of Texas at Austin

Chris Kim

University of Minnesota

Cooperative Institutions

The University of Texas Health Science Center at San Antonio

University at Buffalo, State University of New York

Seoul National University

The University of Texas at Austin

The University of Texas Health Science Center at Houston

The University of Texas MD Anderson Cancer Center

University of Minnesota

Radiation Oncology Associates

Ollscoil na Gaillimhe – University of Galway

Heriot-Watt University

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Distinct roles of XPF-ERCC1 and Rad1-Rad10-Saw1 in replication-coupled and uncoupled inter-strand crosslink repair

Nature Communications (2018)

Ja-Hwan Seol Cory Holland Xiaolei Li Chris Kim Fuyang Li

Yeast Rad1-Rad10 (XPF-ERCC1 in mammals) incises UV, oxidation, and cross-linking agent-induced DNA lesions, and contributes to multiple DNA repair pathways. To determine how Rad1-Rad10 catalyzes inter-strand crosslink repair (ICLR), we examined sensitivity to ICLs from yeast deleted for SAW1 and SLX4, which encode proteins that interact physically with Rad1-Rad10 and bind stalled replication forks. Saw1, Slx1, and Slx4 are critical for replication-coupled ICLR in mus81 deficient cells. Two rad1 mutations that disrupt interactions between Rpa1 and Rad1-Rad10 selectively disable non-nucleotide excision repair (NER) function, but retain UV lesion repair. Mutations in the analogous region of XPF also compromised XPF interactions with Rpa1 and Slx4, and are proficient in NER but deficient in ICLR and direct repeat recombination. We propose that Rad1-Rad10 makes distinct contributions to ICLR depending on cell cycle phase: in G1, Rad1-Rad10 removes ICL via NER, whereas in S/G2, Rad1-Rad10 facilitates NER-independent replication-coupled ICLR.

ERCC1

10.1038/s41467-018-04327-0

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Dynamic DNA binding licenses a repair factor to bypass roadblocks in search of DNA lesions

Nature Communications (2016)

Maxwell W. Brown Yoori Kim Gregory M. Williams John D. Huck Jennifer A. Surtees

DNA-binding proteins search for specific targets via facilitated diffusion along a crowded genome. However, little is known about how crowded DNA modulates facilitated diffusion and target recognition. Here we use DNA curtains and single-molecule fluorescence imaging to investigate how Msh2-Msh3, a eukaryotic mismatch repair complex, navigates on crowded DNA. Msh2-Msh3 hops over nucleosomes and other protein roadblocks, but maintains sufficient contact with DNA to recognize a single lesion. In contrast, Msh2-Msh6 slides without hopping and is largely blocked by protein roadblocks. Remarkably, the Msh3-specific mispair-binding domain (MBD) licences a chimeric Msh2-Msh6(3MBD) to bypass nucleosomes. Our studies contrast how Msh2-Msh3 and Msh2-Msh6 navigate on a crowded genome and suggest how Msh2-Msh3 locates DNA lesions outside of replication-coupled repair. These results also provide insights into how DNA repair factors search for DNA lesions in the context of chromatin.

MSH2

MSH6

Replication protein A

HMG-box

10.1038/ncomms10607

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Citations (52)