期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-13600-9
关键词
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资金
- Natural Science Foundation of China [31870810, 91940302, 91640104, 31670826]
- outstanding youth fund of Zhejiang Province [LR19C050003]
- Fundamental Research Funds for the Central Universities [2017QN81010]
- Zhejiang University
- Austrian Science Fund FWF [P27947, P31691, M2517]
- Austrian Research Promotion Agency FFG (West Austrian BioNMR) [858017]
- Austrian Science Fund (FWF) [M2517] Funding Source: Austrian Science Fund (FWF)
Riboswitches are metabolite-sensing, conserved domains located in non-coding regions of mRNA that are central to regulation of gene expression. Here we report the first three-dimensional structure of the recently discovered S-adenosyl-L-methionine responsive SAM-VI riboswitch. SAM-VI adopts a unique fold and ligand pocket that are distinct from all other known SAM riboswitch classes. The ligand binds to the junctional region with its adenine tightly intercalated and Hoogsteen base-paired. Furthermore, we reveal the ligand discrimination mode of SAM-VI by additional X-ray structures of this riboswitch bound to S-adenosyl-L-homocysteine and a synthetic ligand mimic, in combination with isothermal titration calorimetry and fluorescence spectroscopy to explore binding thermodynamics and kinetics. The structure is further evaluated by analysis of ligand binding to SAM-VI mutants. It thus provides a thorough basis for developing synthetic SAM cofactors for applications in chemical and synthetic RNA biology.
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