Amyloid fibers, those clumps of plaque-like proteins that clog up the brains of Alzheimer's patients, have perplexed scientists with their robust structures. In laboratory experiments, they are able to withstand extreme heat and cold and powerful detergents that cripple most other proteins. The fibers are in fact so tough that researchers now are exploring ways that they can be used in nanoscale industrial applications. While they are not necessarily the cause of Alzheimer's, they are associated with it and with many other neurological conditions, and researchers don't yet have a way to assail these resilient molecules.

A study published this week in the advance online publication of the journal Science suggests that yeast may succeed where scientists have not. The research by a team at Whitehead Institute for Biomedical Research reports on a natural biological process by which yeast cells dismantle amyloid fibers.

"These proteins are remarkably stable," says Susan Lindquist, director of Whitehead and lead researcher on the project. "This is the first time that anyone has found anything that can catalytically take apart an amyloid fiber."

The finding follows years of study that has focused on a yeast protein called Sup35, a protein that helps cells translate genetic information into strings of amino acids the building blocks of protein molecules. Sometimes Sup35 suddenly forms amyloid fibers similar to those found in Alzheimer's patients. In yeast, however, this doesn't kill the cell. Rather, it is part of the cell's normal biology, changing the types of proteins that the cell makes changes that can sometimes be beneficial.

Previous research in the Lindquist lab described how a protein called Hsp104 seemed to affect Sup35's ability to form amyloid fibers. When a yeast cell contained either high amounts of Hsp104 or none at all, amyloid fibers never formed. But when Hsp104 levels were small, the fibers flourished.

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Contact: David Cameron
newsroom@wi.mit.edu
617-258-5183
Whitehead Institute for Biomedical Research
20-May-2004

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