A DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone

Proceedings of the National Academy of Sciences of the United States of America
Sabine MohrAlan M Lambowitz

Abstract

Group II intron RNAs self-splice in vitro but only at high salt and/or Mg2+ concentrations and have been thought to require proteins to stabilize their active structure for efficient splicing in vivo. Here, we show that a DEAD-box protein, CYT-19, can by itself promote the splicing and reverse splicing of the yeast aI5gamma and bI1 group II introns under near-physiological conditions by acting as an ATP-dependent RNA chaperone, whose continued presence is not required after RNA folding. Our results suggest that the folding of some group II introns may be limited by kinetic traps and that their active structures, once formed, do not require proteins or high Mg2+ concentrations for structural stabilization. Thus, during evolution, group II introns could have spliced and transposed by reverse splicing by using ubiquitous RNA chaperones before acquiring more specific protein partners to promote their splicing and mobility. More generally, our results provide additional evidence for the widespread role of RNA chaperones in folding cellular RNAs.

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Citations

Feb 17, 2000·Cellular Signalling·K Ono, J Han
Jul 23, 2011·Nature Reviews. Molecular Cell Biology·Patrick Linder, Eckhard Jankowsky
Dec 18, 2008·Proceedings of the National Academy of Sciences of the United States of America·Yingfeng ChenRick Russell
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