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Updated: May 21, 2026
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RNA Secondary Structure Prediction Using High-throughput SHAPE
Published on: May 31, 2013
Structural flexibility of RNA as molecular basis for Hfq chaperone function
Euripedes de Almeida Ribeiro1, Mads Beich-Frandsen, Petr V Konarev
1Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Nucleic Acids Research
|June 22, 2012
Summary
Host factor Q (Hfq) is an RNA chaperone essential for bacterial gene regulation. This study reveals Hfq
Area of Science:
- Bacterial gene regulation
- RNA-protein interactions
- Structural biology
Background:
- Small regulatory RNAs (sRNAs) are crucial for post-transcriptional gene control in bacteria.
- Host factor Q (Hfq) is an RNA chaperone that facilitates sRNA-mRNA interactions.
- Escherichia coli Hfq (Hfq(Ec)) is a hexameric protein with distinct binding sites for sRNAs and mRNAs.
Purpose of the Study:
- To structurally analyze the complex formed between Hfq(Ec) and a specific sRNA, DsrA.
- To elucidate the role of Hfq structural flexibility in RNA chaperone activity.
Main Methods:
- Small angle X-ray scattering (SAXS)
- Nuclear magnetic resonance (NMR) spectroscopy
- Biochemical assays
Main Results:
- A 1:1 complex of Hfq(Ec) with a DsrA sRNA subsequence (DsrA(34)) was structurally characterized.
- The Hfq(Ec) protein maintained its doughnut structure, while the DsrA(34) RNA exhibited significant flexibility.
- The complex displayed an asymmetric shape in solution.
Conclusions:
- The structural flexibility of RNA bound to Hfq is crucial for its function as an RNA chaperone.
- This flexibility likely facilitates stochastic base pairing between sRNAs and target mRNAs.
- Understanding these interactions provides insights into bacterial gene regulation mechanisms.
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