Read the Publication

This week we profile a recent publication in eLife from John Young (pictured) in the laboratory of Dr. Franck Duong at UBC.

Can you provide a brief overview of your lab’s current research focus?

Our main research focus in the Duong lab is on bacterial membrane proteins. Membrane proteins and complexes play vital roles in many cellular functions, including energy generation, cell division, protein translocation and nutrient import. In many cases, membrane proteins transiently associate with each other into macromolecular complexes in order to carry out their functions. However, despite recent proteomic advances, it is often difficult to identify transient interactors of membrane proteins.

Our current work seeks to address a long-standing problem in the membrane protein proteomics field: How can we improve existing proteomic methods for identifying transient interactions between membrane proteins? Most methods used for studying membrane protein interactions first require the proteins to be extracted from membranes using detergents. However, detergents often disrupt protein structure/function, and dissociate transient interactions. This causes all but the most stable interactions to be lost, and thus undetected.

 What is the significance of the findings in this publication?

We describe a new method – the peptidisc method – for reconstituting the E. coli membrane proteome into detergent-free, water-soluble particles that are amenable to biochemical fractionation. In collaboration with Leonard Foster’s lab at UBC, we combined quantitative proteomics and bioinformatics, and were able to predict a number of novel protein-protein interactions which were not previously identified by other detergent-based methods. We further validated several of these potentially novel interactions by orthogonal biochemical approaches.

What are the next steps for this research?

Our next steps will be to apply the peptidisc method towards studying the membrane proteome of pathogenic bacteria. We’re also looking to extend the method to study the membrane proteome in mammalian systems – stay tuned for our next publications!

Read the Publication