Single-molecule analysis of Mss116-mediated group II intron folding

Krishanthi S. Karunatilaka, Amanda Solem, Anna Marie Pyle () and David Rueda ()
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Krishanthi S. Karunatilaka: Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, USA
Amanda Solem: Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, USA
Anna Marie Pyle: Yale University
David Rueda: Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, USA

Nature, 2010, vol. 467, issue 7318, 935-939

Abstract: Abstract DEAD-box helicases are conserved enzymes involved in nearly all aspects of RNA metabolism, but their mechanisms of action remain unclear. Here, we investigated the mechanism of the DEAD-box protein Mss116 on its natural substrate, the group II intron ai5γ. Group II introns are structurally complex catalytic RNAs considered evolutionarily related to the eukaryotic spliceosome, and an interesting paradigm for large RNA folding. We used single-molecule fluorescence to monitor the effect of Mss116 on folding dynamics of a minimal active construct, ai5γ−D135. The data show that Mss116 stimulates dynamic sampling between states along the folding pathway, an effect previously observed only with high Mg2+ concentrations. Furthermore, the data indicate that Mss116 promotes folding through discrete ATP-independent and ATP-dependent steps. We propose that Mss116 stimulates group II intron folding through a multi-step process that involves electrostatic stabilization of early intermediates and ATP hydrolysis during the final stages of native state assembly.

Date: 2010
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DOI: 10.1038/nature09422

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