Short-lived proteins control gene expression in cells to carry out a number of vital tasks, from helping the brain form connections to helping the body mount an immune defense. These proteins are made in the nucleus and are quickly destroyed once they've done their job. The mechanism degrades short-lived proteins that support brain and immune functions.
Short-lived proteins control gene expression in cells to carry out a number of vital tasks, from helping the brain form connections to helping the body mount an immune defense. These proteins are made in the nucleus and are quickly destroyed once they've done their job.
"The mechanism we found is very simple and quite elegant," added co-lead author Christopher Nardone, a PhD candidate in genetics at HMS."It is a basic science discovery, but there are many implications for the future."It is well established that cells can break down proteins by tagging them with a small molecule called ubiquitin. The tag tells the proteasome that the proteins are no longer needed, and it destroys them.
"What struck me in the beginning is that these proteins are extremely unstable and they have a very short half-life -- once they are produced, they carry out their function, and they are quickly degraded afterwards," Gu said. With the aid of a machine learning tool called AlphaFold that predicts protein structures, plus results from a series of lab experiments, the team was able to flesh out the details of the mechanism. They established that midnolin has a"Catch domain" -- a region of the protein that grabs other proteins and feeds them directly into the proteasome, where they are broken down.
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