A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis

© 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 translocate...

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Main Authors: Chatterjee, Nimrat, D'Souza, Sanjay, Shabab, Mohammad, Harris, Cynthia A, Hilinski, Gerard J, Verdine, Gregory L, Walker, Graham C
Other Authors: Massachusetts Institute of Technology. Department of Biology
Format: Article
Language:English
Published: Wiley 2021
Online Access:https://hdl.handle.net/1721.1/132710
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author Chatterjee, Nimrat
D'Souza, Sanjay
Shabab, Mohammad
Harris, Cynthia A
Hilinski, Gerard J
Verdine, Gregory L
Walker, Graham C
author2 Massachusetts Institute of Technology. Department of Biology
author_facet Massachusetts Institute of Technology. Department of Biology
Chatterjee, Nimrat
D'Souza, Sanjay
Shabab, Mohammad
Harris, Cynthia A
Hilinski, Gerard J
Verdine, Gregory L
Walker, Graham C
author_sort Chatterjee, Nimrat
collection MIT
description © 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.
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spelling mit-1721.1/1327102024-05-31T20:07:35Z A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis Chatterjee, Nimrat D'Souza, Sanjay Shabab, Mohammad Harris, Cynthia A Hilinski, Gerard J Verdine, Gregory L Walker, Graham C Massachusetts Institute of Technology. Department of Biology Koch Institute for Integrative Cancer Research at MIT © 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. 2021-10-04T19:13:57Z 2021-10-04T19:13:57Z 2020-07 2020-05 2021-10-04T17:56:14Z Article http://purl.org/eprint/type/JournalArticle 1098-2280 https://hdl.handle.net/1721.1/132710 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). en 10.1002/EM.22395 Environmental and Molecular Mutagenesis Creative Commons Attribution-Noncommercial-Share Alike http://creativecommons.org/licenses/by-nc-sa/4.0/ application/pdf Wiley PMC
spellingShingle Chatterjee, Nimrat
D'Souza, Sanjay
Shabab, Mohammad
Harris, Cynthia A
Hilinski, Gerard J
Verdine, Gregory L
Walker, Graham C
A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis
title A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis
title_full A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis
title_fullStr A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis
title_full_unstemmed A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis
title_short A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis
title_sort stapled pol κ peptide targets rev1 to inhibit mutagenic translesion synthesis
url https://hdl.handle.net/1721.1/132710
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