Cells produce chaperones that help proteins to fold quickly and correctly. One chaperone, GroEL, has been extensively studied around the world and is used as an example of a chaperone in most biology textbooks.
Jean-François Collet (WEL Research Institute - UCLouvain) and colleagues have discovered that the chaperone GroEL, which was thought to be well known, actually works with Cnox, a chaperedoxin that controls the redox quality of GroEL substrates. The team managed to photograph this interaction between GroEL and its previously unknown partner CnoX.
This unexpected discovery will allow us to better study the way in which proteins survive in the cell, a step forward in understanding the mechanisms involved in diseases such as Alzheimer's or Parkinson's.