Australian researchers make a quantum leap in understanding key cell structures

Researchers in Australia and the UK have made a world first discovery that will provide the most accurate understanding to date of the structure and function of the most important energy converting protein, critical to the function of all organs and a cause of disease when malfunctioning.

Using high-end mass spectrometry, Dr Carol Robinson and her colleagues at Oxford University in the United Kingdom, in collaboration with Dr Daniela Stock at the Victor Chang Cardiac Research Institute (VCCRI) in Australia, determined for the first time how the protein ATP synthase interacts with the critical fatty acids that form the membrane around our cells.

The discovery, published in the illustrious journal Science, will help scientists around the world to understand exactly how ATP synthase is regulated by cell membrane components, and to understand diseases involving ATP synthase, which can affect heart and muscle function as well as heat production and temperature regulation.

Professor Bob Graham, Executive Director at the VCCRI, says this is one of the most important discoveries in basic biological research this year.

“Think of the structure of this protein as being just like a huge rotating turbine that twists and turns to produce electricity.  We have these turbines in every cell of our bodies, which although extremely tiny, are critical for all of our organs to work because they produce required energy.

“For these turbines to work however they need to be lubricated – so each one sits in a membrane made up of lipids or fats, just like a vat of oil.  But just how and how much lubricant is needed for the turbine to function properly, has until now been unknown,” added Professor Graham. 

The paper published today, documents the ground-breaking mass spectrometry method, which was used to determine exactly how much lubricant or fatty acid is attached to the ATP synthase.

“In essence, by analogy, these researchers have weighed the amount of oil or lubrication that’s stuck to the turbine, compared to the turbine itself. This level of accuracy is akin to dumping a person into a big vat of nail polish, and then finding out the exact weight of the nail polish that ends up stuck only to their finger and toenails,” continued Professor Graham.

Professor Graham says knowing how much lubrication is needed for ATP synthase to operate efficiently is critical to understanding how it converts the energy stored in the food we eat for our cells to live and function.

“No one in the world has ever done mass-spectrometry in such a sensitive and sophisticated way before—this is an incredible coup.  While basic in nature, this discovery will aid enormously in the future of applied and clinical research right around the world, as well as helping us understand major diseases caused by defects in our body’s energy converting machinery.”