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Molecular Chaperone Keeps Bacterial Proteins from Slow-Dancing to Destruction

Just like teenagers at a prom, proteins are tended by chaperones whose job it is to prevent unwanted interactions among immature clients. And at the molecular level, just as at the high school gym level, it's a job that usually requires a lot of energy.

In new research, scientists at the University of Michigan and Howard Hughes Medical Institute have discovered how a protein chaperone called HdeA, which helps protect bacteria like the notorious Escherichia coli from the ravages of stomach acid, saves energy while keeping proteins from forming destructive clumps.

The research is described in a paper published online in the Proceedings of the National Academy of Sciences.

Proteins in disease-causing bacteria like E. coli unfold when they land in stomach acid after being accidentally ingested by humans and other animals. This unfolding stops the proteins from working and could spell doom for the bacteria if the chaperone HdeA didn't step in. HdeA works by binding very tightly to the unfolded proteins while the bacteria are in the stomach. By attaching to the bacterial proteins, the chaperone stops them from tangling like slow-dancing teens, which could kill the bacteria.
 
 

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