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Molecular biology: Designer of protein factories exposed
Date:10/24/2013

For 10 years, Patrick Cramer and his colleagues at Ludwig-Maximilians-Universitaet (LMU) in Munich have probed the structure of RNA polymerase I, a crucial cog in the machinery of all cells. Now they unveil the full three-dimensional conformation of the enzyme at atomic resolution.

Actively growing cells must synthesize large amounts of protein, which in turn requires huge numbers of protein production plants, the so-called ribosomes. Ribosomes themselves consist of proteins mounted on a framework of ribosomal RNA. The latter accounts for as much as 60% of the RNA in cells, and is synthesized by the enzyme RNA polymerase I (Pol I). In the absence of ribosomal RNA, no protein synthesis can take place. Pol I is therefore a central pacemaker for cell growth, and aberrant hyperactivation of ribosome biogenesis is a hallmark of many types of cancer.

In spite of its pivotal role in the cell, the structure of the enzyme has remained poorly understood. As a very large and highly complex molecular machine, Pol I has so far proven resistant to conventional high-resolution structural analyses. But in a technical tour-de-force, Professor Patrick Cramer the Director of LMU's Gene Center and his team have now revealed its detailed architecture. In an article in the latest issue of Nature, the researchers describe the complete three-dimensional structure of Pol I at a resolution that not only allows them to localize all of its 14 subunits, but also to define the positions of its approximately 35,000 (non-hydrogen) atoms. The resulting model provides detailed insights into the enzyme's mode of action.

X-rays elucidate crystal structure

"The decisive breakthrough was the result of 10 years of hard work, which taught us how to grow high-quality crystals of the enzyme that were amenable to high-resolution structural analysis by X-ray diffraction. The size and complexity of Pol I made this a very difficult task," as Cramer explains.
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Contact: Luise Dirscherl
dirscherl@lmu.de
49-892-180-2706
Ludwig-Maximilians-Universitt Mnchen
Source:Eurekalert

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