Scientists at the Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC) have discovered that the protein Urm1 protects other proteins in stress situations and thus ensures that cells can survive under extreme conditions. Cells are constantly exposed to stress, such as heat, cold, or oxidative stress. To survive, cells have developed a variety of protective mechanisms, including the production of heat shock proteins. These proteins help to stabilize other proteins and prevent them from being damaged by stress.

The research team led by Dr. Matthias Seedorf and Dr. Frank Buchholz has now discovered that the protein Urm1 plays a key role in the production of heat shock proteins. Urm1 is a chaperone, which means that it helps other proteins to fold into their correct shape. The researchers found that Urm1 binds to the messenger RNA (mRNA) of heat shock proteins and helps to recruit ribosomes to the mRNA, which is necessary for the production of proteins.

In the absence of Urm1, the production of heat shock proteins is impaired and cells are more sensitive to stress. The researchers also found that Urm1 is essential for the survival of cells under extreme stress conditions.

These findings provide new insights into the mechanisms that cells use to protect themselves from stress. The discovery that Urm1 plays a key role in heat shock protein synthesis opens up new possibilities for the development of therapies for stress-related diseases.