Studying RNA enzymes. The graph in the foreground shows how the enzymes catalytic activity is related to the rates at which the molecule folds and unfolds. These rates were measured by single-molecule fluorescence microscopy, where individual molecules light up as bright spots shown in the background. Also depicted, top right, is a ribbon-and-stick representation of the crystal structure of the folded RNA enzyme.
Research aimed at teasing apart the workings of RNA enzymes eventually may lead to ways of monitoring fat metabolism and might even assist in the search for signs of life on Mars, according to University of Michigan researcher Nils Walter. His latest work was published online in the Proceedings of the National Academy of Sciences June 24.
Walter and associates at U-M and colleague Xiaowei Zhuang and associates at Harvard University, use techniques that allow them to study single molecules of RNA enzymes, also known as ribozymes. Like the more familiar protein enzymes, RNA enzymes accelerate chemical reactions inside cells. Researchers want to learn how changes in ribozyme molecules affect their activity, both to better understand how evolution has shaped ribozymes to carry out their duties and to find ways of manipulating them for useful purposes.
In the recent research, Walter’s group combined a technique called single-molecule fluorescence resonance energy transfer (FRET) with mathematical simulations to study a ribozyme involved in the replication of a tobacco-infecting virus. Just as a protein enzyme is not a static structure, a ribozyme also changes shape, cycling back and forth between its compact, catalytically active form and its inactive, extended form. Single-molecule FRET allowed the researchers to directly observe and measure how quickly the ribozyme switched forms and how these rates changed when various parts of the molecule were altered.
Nancy Ross Flanigan | EurekAlert!
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