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Nucleotide flipping correlates with fluorescence activation in the RhoBAST imaging platform
Xiaoqing Tai1, Mengqi He1, Christoph Mitteregger2
1Department of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China.
Nature Communications
|July 21, 2026
Summary
Super-resolution imaging is enhanced by the RhoBAST fluorogenic RNA aptamer. Its unique structure and nucleotide flipping mechanism enable faster ligand turnover and fluorescence flickering for advanced RNA dynamics studies.
Area of Science:
- Molecular Biology
- Biophysics
- Structural Biology
Background:
- Fluorogenic RNA aptamers are crucial for super-resolution imaging.
- Understanding their photophysical properties is key to improving RNA dynamics studies.
Purpose of the Study:
- Determine the structure of RhoBAST and its ligand-bound complexes.
- Elucidate the molecular mechanism behind RhoBAST's imaging capabilities.
Main Methods:
- X-ray crystallography to determine free-form and ligand-bound structures.
- Mutagenesis studies.
- Biophysical assays including fluorescence spectroscopy and surface plasmon resonance.
Main Results:
- RhoBAST exhibits an inverted 'V'-shaped architecture.
- Ligand binding induces a conformational flip in nucleotide G38.
- This nucleotide flipping facilitates rapid ligand turnover and fluorescence flickering.
Conclusions:
- A novel nucleotide-flipping mechanism in fluorogenic RNA aptamers is identified.
- Structural and mechanistic insights provide a blueprint for designing next-generation RNA imaging tools.
