What do you believe is the single most important factor driving up the cost of living in Nigeria?

Proteins control most of the body's functions, and their malfunction can have severe consequences, such as neurodegenerative diseases or cancer. Therefore, cells have mechanisms in place to control protein quality.

In animal and human cells, chaperones of the Hsp70 class are at the heart of this control system, overseeing a wide array of biological processes. Yet, despite their crucial role, the precise molecular mechanism of Hsp70 chaperones has remained elusive for decades.

Using a cutting-edge nanopore single-molecule technique, a team from the University of Geneva (UNIGE), in collaboration with EPFL, has now made a significant breakthrough in determining how Hsp70 chaperones generate the force needed to manipulate the structure of their client proteins. These results, which put an end to a decade of debate, are published in Nature Communications.

Proteins need to fold into specific three-dimensional shapes to function correctly. Among their several roles, chaperone proteins like Hsp70s typically assist the correct folding of proteins. To successfully perform these tasks, Hsp70s need to forcefully manipulate the structure of the proteins, extracting them from aggregates that had formed spontaneously or by facilitating protein translocation into key cell compartments, such as mitochondria.

In this context, during the 1990s and early 2000s, there was an intense debate about the mechanism allowing Hsp70 chaperones to drive protein translocation, with two main models proposed based on different sets of experiments, but with no definitive answer.

• Read More