A Toxic Tragedy: The Molecular Story of the Toxin YafQ's Regulation of Protein Translation

Abstract

As part of the CREST3 (Connecting Researchers, Educators and STudents) program, undergraduate students from the University of Minnesota Rochester's ASBMB student chapter designed a novel three‐dimensional physical model representing the molecular story of how the protein toxin YafQ regulates protein translation. During times of cellular stress, Escherichia coli uses YafQ, an mRNA interferase, to prevent protein translation. Here, the cell activates the toxin by degrading an antitoxin protein (DinJ), which is normally bound to the toxin when no cellular stress is present. After dissociation of DinJ, YafQ is able to bind to the entrance site of the ribosome and catalyze hydrolysis of the mRNA strand which effectively degrades the mRNA strand and halts transcription. Based on this information, we designed a physical model demonstrating how the mRNA is able to bind to YafQ once DinJ dissociates. In order to ensure the proper orientation and proximity of the mRNA within our model, we utilized AutoDock Vina to dock an mRNA analog AAA (Ligand ID: 25A) to YafQ (PDB ID: 4Q2U). In this presentation we will demonstrate how to design and use a physical model to tell a molecular story based on biochemical data from the literature.This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.