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CAREER: The Role of Nep1 in Ribosome Biogenesis

$1,088,972FY2010BIONSF

University Of Maryland, College Park, College Park MD

Investigators

Abstract

Intellectual Merit The synthesis of new ribosomes, the cell's protein producing machinery, is an energetically costly and highly regulated process. It is also a dynamic process that requires molding of the RNA and binding of ribosomal proteins into the final functional three-dimensional structure of the ribosome. The complexity and importance of producing ribosomes requires that multiple accessory factors guide and regulate processing. This project focuses on a ribosome processing factor, Nep1, a protein required for the proper assembly and maturation of the small subunit of the ribosome. The studies address the mechanism by which Nep1 guides the binding of the ribosomal protein S19 into the small subunit of the yeast ribosome, and the changes in RNA structure that occur as a result. The results of this project will provide a more detailed molecular understanding of Nep1 function, and more broadly, address the role of RNA dynamics in ribosome assembly. Broader Impact Training in structural biology and an understanding of molecular structure provides scientists with a roadmap to important biological questions. The educational portion of this project will focus on training university students in structure-based approaches to biological and biochemical research, and providing the necessary skills to produce macromolecular crystals. Structural biology, especially using macromolecular X-ray crystallography, is fairly embryonic at University of Maryland at College Park, and there is much interest on campus for incorporating structural approaches in research. To meet that interest and enhance education in this area, this project will incorporate a yearly workshop in practical macromolecular crystallography for students who are interested in generating X-ray crystal structures as part of their research. This will allow the research community to utilize excellent on-campus facilities for structural data collection and firmly establish structural biology research at this university.

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