The p53 protein can determine whether a cell lives or dies. If genetic damage is detected, the protein promotes apoptosis. New research from the University of California medical school shows that this cancer defense only works in the presence of special proteins called molecular chaperones.
In many cancer treatments, not only do they attack cancer cells, they also damage normal cells. So finding a healthier way is a medical dream.P53 can be studied as a naturally harmless therapeutic direction. The presence of p53 serves as a monitoring function, and when severe genomic damage is detected, the cell initiates a process of apoptosis, which prevents tumor cell growth.
But how does this regulatory mechanism work？To answer this question, the scientists tagged p53 with a fluorescent dye to monitor the structure of individual p53 molecules. In an isolated state, p53 presents a folding pattern and is fully unfolded under the influence of Hsp70, consuming energy in this process. When Hsp90 is added, the expanded p53 returns to its folded form again.
"Molecular chaperones play a significant role in the morphology and function of p53," the researchers lamented. "Cells have an extremely complex regulatory mechanism, and molecular chaperones play a guiding role in the correct alignment of tumor suppressor proteins."
Molecular chaperones on the one hand keep p53 unfolded and bioactive. But if the cell is stressed, the chaperone causes p53 to fold, bind to the DNA, and even cause the cell itself to die.
The researchers believe this pattern of molecular interactions could lead to a better understanding of how proteins work and could lead to new targets for cancer treatment.