Medical School researchers published the results of an enzyme study last month which may eventually lead to a better understanding of the processes behind early-aging diseases and to redesigned AIDS medications with fewer negative side effects.
Researchers from the Center for Membrane Biology analyzed the yeast enzyme Ste24p, whose properties are biochemically similar to a protein found in humans that is responsible for the formation of a healthy cell’s nuclear structure. The team was able to determine the exact structure of the enzyme and subsequently develop a better understanding of why it malfunctions.
Protein Ste24p was first discovered in yeast specimens that were unable to reproduce — hence the protein’s official name of Sterile-24p. The human counterpart of the membrane protein, ZmpSte24, is responsible for creating Lamin A, a structural, mesh-like protein that gives the nuclear membrane of a human cell its structure. This membrane encapsulates the nucleus’ genetic material. Ineffective or nonexistent Lamin A production can result in rare early-aging diseases such as progeria, a rare condition that causes children to age prematurely.
“Learning about the yeast structure will help us understand the human protein,” researcher Edward Pryor said. “There are implications for understanding the aging process in humans.”
Discovering the structure of Ste24p will also help improve treatment practices of individuals with HIV. Patients are often treated with HIV protease inhibitors, which prevent the yeast Ste24p protein and the human ZmpSte24 protein from working. This can lead to degenerative conditions, altered fat metabolism, insulin resistance and diabetes.
Pryor said the better understanding of the protein’s structure will help future researchers develop HIV drugs without these side effects.
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