As part of our WCMR Science Seminar Series, we recently heard from PhD student Matt Zorkau who talked about his research project that aims to better understand how and where mitochondrial proteins are made within cells. To do this, Matt has developed a novel way to visualise newly made mitochondrial proteins using high resolution fluorescence microscopy. Read on to find out more.

One of the key functions of mitochondria is creating a usable energy source for the cell. They achieve this through activity of oxidative phosphorylation (OXPHOS) complexes, which consist of proteins (building blocks) that are synthesised in both the nucleus and the mitochondria themselves. Mutations in the genes that encode for these OXPHOS proteins can lead to mitochondrial disease. The goal of my work is to better understand how mitochondrial protein synthesis is normally coordinated in cells and how this is affected in disease.

To address this, I have developed a novel method to visualise and measure where newly made mitochondrial proteins are located by high resolution fluorescence microscopy. The technique is less expensive, simpler to use and provides an increased amount of information compared to current methods that measure mitochondrial protein synthesis. This potentially provides advantages in basic research, mitochondrial disease diagnostics and drug screening for treatments.

Some of the important discoveries I have made so far concern the distribution of mitochondrial protein synthesis in healthy and patient cells, as well as characterising exactly where within individual mitochondria the proteins are made. Overall, the project provides a new platform for investigating some of the crucial steps for mitochondria to function correctly. Improving understanding in this area could lead to better diagnostics and treatments for sufferers of mitochondrial disease.

The super resolution microscopy image above shows where mitochondrial protein synthesis (green) is located within human mitochondria (outlined in red).

To find out more about Matt’s research project, click here.