Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

A DEAD-Box Protein Alone Promotes Group II Intron Splicing and Reverse Splicing by Acting as an RNA Chaperone

Sabine Mohr, Manabu Matsuura, Philip S. Perlman and Alan M. Lambowitz
Proceedings of the National Academy of Sciences of the United States of America
Vol. 103, No. 10 (Mar. 7, 2006), pp. 3569-3574
Stable URL: http://www.jstor.org/stable/30048628
Page Count: 6
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
A DEAD-Box Protein Alone Promotes Group II Intron Splicing and Reverse Splicing by Acting as an RNA Chaperone
Preview not available

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 al5γ and bll group II introns under near-physiological conditions by acting as an ATPdependent 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.

Page Thumbnails

  • Thumbnail: Page 
3569
    3569
  • Thumbnail: Page 
3570
    3570
  • Thumbnail: Page 
3571
    3571
  • Thumbnail: Page 
3572
    3572
  • Thumbnail: Page 
3573
    3573
  • Thumbnail: Page 
3574
    3574