he mutant gene worked. He found that a slightly altered tail structure prevented the S14 protein from "cutting" its target RNA molecule, thus halting ribosome assembly. Because it wasn't processed, this typically short-lived RNA molecular intermediate accumulated within yeast cells, making it easy to isolate and study. Yeast engineered with mutations in genes for other proteins that direct ribosome assembly should yield even more intermediates for study, according to Woolford, whose research was supported by the National Institutes of Health and reported in the May 7 issue of Molecular Cell.
In collaboration with Martin Farach-Colton at Rutgers University, Woolford is currently developing computer models to outline the many proteins involved in ribosome assembly and the step-by-step process by which various parts come together to make a new ribosome. In addition, Woolford is carrying out genetic experiments to test their idea that certain non-ribosomal proteins that regulate ribosome assembly (called ribosomal assembly factors) also regulate cell proliferation.
"We think that specific ribosome assembly factors we discovered might have a second 'moonlighting' job," said Woolford. "Thus, if such a protein functions in both ribosome assembly and growth regulation, cells could coordinate these two processes by 'talking' to the same molecule in two places."
In this scenario, if a cell told a ribosome assembly factor to stop working, it would effectively shut down ribosome production and at the same time trigger cells to stop dividing. But if that factor failed to hear what the cell dictated, it would continue to build ribosomes and spur cell division that could lead to cancer, according to Woolford.
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Contact: Lauren Ward
Carnegie Mellon University
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