Collaborations between Johns Hopkins and National Taiwan University researchers have successfully manipulated the life span of common, single-celled yeast organisms by figuring out how to remove and restore protein functions related to yeast aging. A chemical variation of a "fuel-gauge" enzyme that senses energy in yeast acts like a life span clock: It is present in young organisms and progressively diminished as yeast cells age. The discovery reveals molecular components of an aging pathway that appears related to one that regulates longevity and lifespan in humans. Scientists believe they now have a biochemical route to youth that does not involve the diet. The chemical variation, known as acetylation because it adds an acetyl group to an existing molecule, is a kind of "decoration" that goes on and off a protein. Acetylation can profoundly change protein function in order to help an organism or system adapt quickly to its environment. Until now, acetylation had not been directly implicated in the aging pathway, so this is an all-new role and potential target for prevention or treatment strategies. The normal replicative lifespan in natural yeast is 25. In the yeast genetically modified by researchers to restore the chemical modification, life span extended to 38, an increase of about 50 percent. With these new discoveries, further research will most likely be done to see how this "anti-aging" can apply to humans.
As "anti-aging" has increased the lifespan of the yeast cells through the removing and reintroduction of the protein acetylation, could further proteins be added to potentially create 2 and 3 fold life span increases in bacterial organisms that generally have an already long lifespan, or is there a certain threshold dependent on the species and condition of the reintroduced protein?
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