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Protein-Facilitated Ribozyme Folding and Catalysis
Author(s) -
Nora Zingler,
Amanda Solem,
Anna Marie Pyle
Publication year - 2008
Publication title -
nucleic acids symposium series
Language(s) - English
Resource type - Journals
eISSN - 1746-8272
pISSN - 0261-3166
DOI - 10.1093/nass/nrn034
Subject(s) - ribozyme , protein folding , folding (dsp implementation) , chemistry , hairpin ribozyme , biophysics , computational biology , microbiology and biotechnology , biology , biochemistry , rna , gene , electrical engineering , engineering
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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