JD Rubin

University of Colorado Boulder

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DJ Taatjes

University of Colorado Boulder

Cecilia B. Levandowski

University of Colorado Boulder

Alanna Schepartz

University of California, Berkeley

Timothy Read

Emory University

Kaiseng Quach

RWTH Aachen University

BL Allen

University of Colorado Boulder

RD Dowell

University of Colorado Boulder

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University of Colorado Boulder

University of Colorado System

University of Cincinnati

Duke University

George Mason University

University of North Carolina at Chapel Hill

Memorial Sloan Kettering Cancer Center

University of Colorado Anschutz Medical Campus

University of Colorado Denver

University of California, San Diego

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Suppression of p53 response by targeting p53-Mediator binding with a stapled peptide

bioRxiv (Cold Spring Harbor Laboratory) (2019)

BL Allen Kaiseng Quach Cecilia B. Levandowski JD Rubin Timothy Read

Abstract DNA-binding transcription factors (TFs) remain challenging to target with molecular probes. Many TFs function in part through interaction with Mediator; we sought to block p53 function by disrupting the p53-Mediator interaction. Through rational design and activity-based screening, we characterized a stapled peptide, with functional mimics of both p53 activation domains, that selectively inhibited p53- and Mediator-dependent transcription in vitro . This “bivalent peptide” also suppressed p53 transcriptional response in human cancer cells. Our strategy circumvents the TF and instead targets the TF-Mediator interface, with desired transcriptional outcomes. Different TFs target Mediator through different subunits, suggesting this strategy could be broadly applied.

Mediator

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10.1101/757401

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