NDLI: Increased Ribozyme Activity in Crowded Solutions

Content Provider	Journal of Biological Chemistry (JBC)
Author	Desai, Ravi Kilburn, Duncan Lee, Hui-Ting Woodson, Sarah A.
Abstract	Noncoding RNAs must function in the crowded environment of the cell. Previous small-angle x-ray scattering experiments showed that molecular crowders stabilize the structure of the Azoarcus group I ribozyme, allowing the ribozyme to fold at low physiological Mg2+ concentrations. Here, we used an RNA cleavage assay to show that the PEG and Ficoll crowder molecules increased the biochemical activity of the ribozyme, whereas sucrose did not. Crowding lowered the Mg2+ threshold at which activity was detected and increased total RNA cleavage at high Mg2+ concentrations sufficient to fold the RNA in crowded or dilute solution. After correcting for solution viscosity, the observed reaction rate was proportional to the fraction of active ribozyme. We conclude that molecular crowders stabilize the native ribozyme and favor the active structure relative to compact inactive folding intermediates.
Related Links	http://www.jbc.org/content/289/5/2972.abstract
Ending Page	2977
Starting Page	2972
Page Count	6
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	5
Volume Number	289
DOI	10.1074/jbc.M113.527861
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2014-01-31
Access Restriction	Open
Subject Keyword	Macromolecular Crowding Ribozyme RNA Catalysis RNA Folding X-ray Scattering PEG Molecular Biophysics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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