Structural prediction of Ypq1 – UROP Spring Symposium 2021

Structural prediction of Ypq1

Victoria O’Donnell


Pronouns: She/Her

Research Mentor(s): Ming Li, Assistant Professor
Research Mentor School/College/Department: Molecular, Cellular, and Developmental Biology, College of Literature, Science, and the Arts
Presentation Date: Thursday, April 22, 2021
Session: Session 6 (4pm-4:50pm)
Breakout Room: Room 8
Presenter: 3

Event Link


The cell responds to changes in its environment by changing the protein composition on the plasma membrane (PM). Many proteins are regulated based on their substrate concentration, including the lysine importer on the vacuole membrane (VM) of yeast, Ypq1. While it is well known that E3 ubiquitin ligases selectively ubiquitinated proteins in response to environmental cues, the mechanisms of this selectivity are poorly understood, particularly in the transmembrane region. Ssh4 is the yeast E3 ligase adapter that recruits Ssh4, the ubiquitin ligase, to the membrane. Ssh4 selectively recognizes Ypq1 in a lysine depleted environment. However, the structures of Ypq1 and Ssh4 are not solved. We used homology modeling and docking prediction programs to generate predicted structures of Ypq1 and Ssh4. Predicted models are useful for providing estimates of locations of critical regions of each protein, such as the active site of Ypq1, ubiquitination sites, and the interaction sites between Ssh4 and Ypq1.

Authors: Victoria O’Donnell
Research Method: Laboratory Research

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