Scientists watch, molecule by molecule, as cell helpers rescue problem proteins
University of Wollongong (UOW) scientists have uncovered, for the first time, exactly how two of the cell's "helper" proteins operate as a rescue crew for misfolded proteins, a discovery that sheds new light on the molecular breakdown that underpins neurodegenerative diseases.
For the first time, researchers at the University of Wollongong (UOW) have observed how two special protein helpers, heat shock protein 70 (Hsp70) and Hsp90, work together to rescue misfolded proteins, a discovery that offers new insights into neurodegenerative diseases. Utilizing ultra-sensitive imaging, the team watched these chaperone proteins in real-time as they helped a fluorescent protein called luciferase fold into its proper three-dimensional structure.
Proper protein folding is crucial for biological function, and when proteins misfold, they can clump together, leading to cell damage that is strongly associated with diseases such as motor neuron disease, Alzheimer's, and Parkinson's. The study, published in Science Advances, showed that Hsp90 can rescue proteins stuck in a nonfunctional state by Hsp70, giving them another chance to fold correctly.
This marks the discovery of a previously unknown coordination system where one chaperone manages another's tendency to hold onto a protein too tightly, ensuring successful folding even under unfavorable conditions. By revealing how cells naturally prevent protein misfolding and clumping, this research opens new possibilities for developing therapies to improve the lives of those affected by conditions linked to protein damage.
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