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Nucleic Acids Symposium Series 2008 52(1):67-68; doi:10.1093/nass/nrn034
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© 2008 Oxford University Press

This article appears in the following Nucleic Acid Symposium Series issue: Joint Symposium of the 18th International Roundtable on Nucleosides, Nucleotides and Nucleic Acids and the 35th International Symposium on Nucleic Acids Chemistry [View the issue table of contents]

Protein-Facilitated Ribozyme Folding and Catalysis

Nora Zingler2,*, Amanda Solem2 and Anna Marie Pyle1,2

1Howard Hughes Medical Institute and 2Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA

*Corresponding Author. E-mail: nora.zingler{at}yale.edu

Abstract

In vivo, large RNAs rely on proteins to fold to their native conformation. In the case of the S. cerevisiae group II intron ai5{gamma}, the DEAD-box protein Mss116 has been shown to promote the formation of the catalytically active structure. However, it is a matter of debate whether it does this by stabilizing on-pathway intermediates or by disrupting misfolded structures. Here we present the available experimental evidence to distinguish between those mechanisms and discuss the possible interpretations.


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