Toward predicting self-splicing and protein-facilitated splicing of group I introns

  1. Quentin Vicens1,
  2. Paul J. Paukstelis2,
  3. Eric Westhof3,
  4. Alan M. Lambowitz2, and
  5. Thomas R. Cech1
  1. 1Howard Hughes Medical Institute, University of Colorado, Department of Chemistry and Biochemistry, Boulder, Colorado 80309-0215, USA
  2. 2Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, and Section of Molecular Genetics and Microbiology, School of Biological Sciences, University of Texas at Austin, Austin, Texas 78712, USA
  3. 3Institut de Biologie Moléculaire et Cellulaire du CNRS, Université Louis Pasteur, F-67084 Strasbourg Cedex, France

Abstract

In the current era of massive discoveries of noncoding RNAs within genomes, being able to infer a function from a nucleotide sequence is of paramount interest. Although studies of individual group I introns have identified self-splicing and nonself-splicing examples, there is no overall understanding of the prevalence of self-splicing or the factors that determine it among the >2300 group I introns sequenced to date. Here, the self-splicing activities of 12 group I introns from various organisms were assayed under six reaction conditions that had been shown previously to promote RNA catalysis for different RNAs. Besides revealing that assessing self-splicing under only one condition can be misleading, this survey emphasizes that in vitro self-splicing efficiency is correlated with the GC content of the intron (>35% GC was generally conductive to self-splicing), and with the ability of the introns to form particular tertiary interactions. Addition of the Neurospora crassa CYT-18 protein activated splicing of two nonself-splicing introns, but inhibited the second step of self-splicing for two others. Together, correlations between sequence, predicted structure and splicing begin to establish rules that should facilitate our ability to predict the self-splicing activity of any group I intron from its sequence.

Keywords

Footnotes

  • Reprint requests to: Quentin Vicens, Howard Hughes Medical Institute, University of Colorado, UCB 215, Department of Chemistry and Biochemistry, Boulder, CO 80309-0215, USA; e-mail: quentin.vicens{at}colorado.edu; fax: (303) 492-6194.

  • Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.1027208.

    • Received February 2, 2008.
    • Accepted July 8, 2008.
  • Freely available online through the open access option.

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