A critical assessment of the utility of protein-free splicing systems

  1. Duncan J. Smith and
  2. Maria M. Konarska
  1. Laboratory of Molecular Biology and Biochemistry, The Rockefeller University, New York, New York 10065, USA

Abstract

U2 and U6 snRNAs form part of the catalytic spliceosome and represent strong candidates for components of its active site. Over the past decade it has become clear that these snRNAs are capable of catalyzing several different chemical reactions, leading to the widespread conclusion that the spliceosome is a ribozyme. Here, we discuss the advances in both protein-free and fully spliceosomal systems that would be required to conclude that the reactions observed to be catalyzed by protein-free snRNAs are related to splicing and question the reliability of snRNA-only systems as tools for mechanistic splicing research.

Keywords

Footnotes

  • Reprint requests to: Maria M. Konarska, Laboratory of Molecular Biology and Biochemistry, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA; e-mail: konarsk{at}mail.rockefeller.edu; fax: (212) 327-7147.

  • Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.1322709.

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