Previously, scientists thought that Hsps could only prevent proteins from aggregating as temperatures rise. But now, Susan Lindquist , Ph.D., and colleague John Glover, Ph.D., have shown that protein snarls can actually be rescued by Hsp104 with the assistance of two other heat shock proteins.
Heat is a protein's enemy.
As an egg fries, its proteins, which are made of chains of molecules called amino acids precisely folded into spirals, loops and sheets, begin to loose their shape. In the body, heat stress can do the same thing to proteins, making them dysfunctional. We thought that Hsps bind to sticky surfaces presented by denatured proteins to prevent them from interacting and forming a blob, and they do. But now we have shown that at least one heat shock protein, namely Hsp104, has the ability to rescue proteins that have already aggregated. This ability is essential to the survival of cells facing extreme heat.