New Assay Reveals Biophysical Properties That Allow Certain Proteins to Infect Others
Proteins are essential workhorses of cells and have many roles, from providing structural support to catalyzing almost all of the chemical reactions that must occur for the organism to survive. A protein’s function is dictated by its three-dimensional shape. However, a prion protein will sometimes transform itself into a different shape that “infects” other proteins by templating them to adopt the alternate shape. In some cells and tissues, prion accumulations disrupt normal functions and lead to disease. In other cells, however, prion self-assemblies are essential for their normal functions.
How and why do some proteins exhibit prion behavior? Researchers from the Halfmann Lab have identified a physical basis for the transformation. They describe the development of a new technique called Distributed Amphifluoric FRET that measures nucleation—the first step in the transformation—in living cells. The assay can distinguish between proteins that exhibit prion behavior and those that do not. This approach may help researchers understand more about prions associated with diseases as well as prions involved in normal biological processes.
The research was published in the July 5, 2018, issue of Molecular Cell.