Related Experiment Video
Updated: Dec 17, 2025

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
A stapled POL κ peptide targets REV1 to inhibit mutagenic translesion synthesis
Nimrat Chatterjee1, Sanjay D'Souza1,2, Mohammad Shabab1
1Department of Biology, MIT, Cambridge, Massachusetts, USA.
Abstract:
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.
Related Concept Videos
Translesion DNA Polymerases
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
Conservative Site-specific Recombination and Phase Variation
The recognition sites for Cre recombinase called LoxP...
Restarting Stalled Replication Forks
Homologous Recombination
DNA Damage can Stall the Cell Cycle
DNA Damage Can Stall the Cell Cycle

