Journal
NATURE
Volume 467, Issue 7318, Pages 935-U75Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature09422
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Funding
- National Institutes of Health [R01GM085116, R01GM050313]
- National Science Foundation [MCB-0747285]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0747285] Funding Source: National Science Foundation
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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 ai5 gamma. 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, ai5 gamma-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.
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