Overbeck, Jan H. and Vogele, Jennifer and Nussbaumer, Felix and Duchardt-Ferner, Elke and Kreutz, Christoph and Wohnert, Jens and Sprangers, Remco (2023) Multi-Site Conformational Exchange in the Synthetic Neomycin-Sensing Riboswitch Studied by 19 F NMR. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 62 (23). ISSN 1433-7851, 1521-3773
Full text not available from this repository. (Request a copy)Abstract
The synthetic neomycin-sensing riboswitch interacts with its cognate ligand neomycin as well as with the related antibiotics ribostamycin and paromomycin. Binding of these aminoglycosides induces a very similar ground state structure in the RNA, however, only neomycin can efficiently repress translation initiation. The molecular origin of these differences has been traced back to differences in the dynamics of the ligand:riboswitch complexes. Here, we combine five complementary fluorine based NMR methods to accurately quantify seconds to microseconds dynamics in the three riboswitch complexes. Our data reveal complex exchange processes with up to four structurally different states. We interpret our findings in a model that shows an interplay between different chemical groups in the antibiotics and specific bases in the riboswitch. More generally, our data underscore the potential of F-19 NMR methods to characterize complex exchange processes with multiple excited states.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RELAXATION DISPERSION; CHEMICAL-EXCHANGE; PROTEIN STATES; EXCITED-STATES; NUCLEIC-ACIDS; INTERMEDIATE; SPECTROSCOPY; DOMAIN; DYNAMICS; PATHWAY; Aminoglycosides; F-19 NMR; NMR Spectroscopy; RNA Dynamics |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Remco Sprangers |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 12 Mar 2024 10:39 |
| Last Modified: | 12 Mar 2024 10:42 |
| URI: | https://pred.uni-regensburg.de/id/eprint/59721 |
Actions (login required)
 |
View Item |
