A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis
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nihms-1690326.pdf
Description
Accepted version
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619.56 KB
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Author(s)
Chatterjee, Nimrat
D'Souza, Sanjay
Shabab, Mohammad
Harris, Cynthia A
Hilinski, Gerard J
Verdine, Gregory L
Walker, Graham C
Date Issued
July 2020
Journal
Environmental and Molecular Mutagenesis
Publisher
Wiley
Citation
Chatterjee, Nimrat, D'Souza, Sanjay, Shabab, Mohammad, Harris, Cynthia A, Hilinski, Gerard J et al. 2020. "A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis." Environmental and Molecular Mutagenesis, 61 (8).
Version
Author's final manuscript
Abstract
© 2020 Wiley Periodicals LLC Stapled α-helical RIR (Rev1-interacting region) peptides of DNA POL κ bind more effectively to the RIR-interface of the C-terminal recruitment domain of the translesion synthesis DNA polymerase Rev1 than unstapled peptide. The tightest-binding stapled peptide translocates into cells and enhances the cytotoxicity of DNA damaging agents while reducing mutagenesis. Drugs with these characteristics could potentially serve as adjuvants to improve chemotherapy and reduce acquired resistance by inhibiting Rev1-dependent mutagenic translesion synthesis.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Koch Institute for Integrative Cancer Research at MIT
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Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1002/EM.22395
