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A 'dimmer switch' for genes

ual decline in DNA binding, gradually turning a gene off.

"One thing we didn't get was why Ets-1 worked differently before and after phosphorylation [the addition of phosphate]," says Pufall, "because as far as we could tell, the overall shape of the molecule didn't change."

"A protein molecule is not like a rock. It's more like Jell-O: it has structure, it has shape, but it jiggles," explains Graves. "We didn't discover jiggling, but we were able to determine that the amount of internal motion within a protein corresponds to the ability of a protein to do its work." Phosphorylation was found to decrease the internal motion of Ets-1, reducing its activity.

According to Pufall, "Ets-1 provides a remarkable illustration of how elegantly proteins are put together ?forming a distinct shape, but with the versatility to respond to the changing needs of the cell, however subtle."

The findings have long-term implications for the study of all proteins, because, according to Graves, any protein has the potential to be organized this way, with structured and unstructured regions that work together.


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Source:Huntsman Cancer Institute/University of Utah Health Sciences Center


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