Proteins folding badly: havoc ensues

When exposed to the antibiotic streptomycin, bacterial cells begin making mistakes in protein production. The error-ridden proteins fold improperly and accumulate in the cell, clumping into toxic aggregates that eventually kill the bacteria.

Such aggregates are of broad interest because they are also a hallmark of neurodegenerative conditions such as Alzheimer’s disease. A research group led by Dieter Söll, Ph.D., Sterling Professor of Molecular Biophysics and Biochemistry and professor of chemistry, Jesse Rinehart, Ph.D., assistant professor of cellular and molecular physiology, and Jiqiang Ling, Ph.D., postdoctoral associate, have found that proteins misfolded due to streptomycin are unusually prone to oxidation, a chemical state more likely to damage the bacterial cell. When the group amplified the expression of certain genes related to oxidation and reduction, streptomycin induced far less damage.

The results, published in the December 14, 2012 issue of Molecular Cell, could shed light on protein aggregates related to human disease.


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