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Updated: Jun 28, 2026
An Assay for Quantifying Protein-RNA Binding in Bacteria
Published on: June 12, 2019
A phage RNA-binding protein binds to a non-cognate structured RNA and stabilizes its core structure
Mao-Hua Xie1, Qi-Jia Wu, Yan-Fei Jiang
1State Key Laboratory of Virology and Department of Biotechnology, College of Life Sciences, Wuhan University, Wuhan, Hubei 430072, China.
Abstract:
Recent studies suggest that some RNA-binding proteins facilitate the folding of non-cognate RNAs. Here, we report that bacteriophage MS2 coat protein (MS2 CP) bound and promoted the catalytic activity of Candida group I ribozyme. Cloning of the MS2-bound RNA segments showed that this protein primarily interacts with the P5ab-P5 structure. Ultraviolet cross-linking and the T1 footprinting assay further showed that MS2 binding stabilized tertiary interactions, including the conserved L9-P5 interaction, and led to a more compact core structure. This mechanism is similar to that of the yeast mitochondrial tyrosyl-tRNA synthetase on other group I introns, suggesting that different RNA-binding proteins may use common mechanisms to support RNA structures.
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