Overbeck, Jan H. and Stelzig, David and Fuchs, Anna-Lisa and Wurm, Jan Philip and Sprangers, Remco (2022) Observation of conformational changes that underlie the catalytic cycle of Xrn2. NATURE CHEMICAL BIOLOGY, 18 (10). pp. 1152-1160. ISSN 1552-4450, 1552-4469
Full text not available from this repository. (Request a copy)Abstract
Nuclear magnetic resonance (NMR) methods that quantitatively probe motions on molecular and atomic levels have propelled the understanding of biomolecular processes for which static structures cannot provide a satisfactory description. In this work, we studied the structure and dynamics of the essential 100-kDa eukaryotic 5' -> 3' exoribonuclease Xrn2. A combination of complementary fluorine and methyl-TROSY NMR spectroscopy reveals that the apo enzyme is highly dynamic around the catalytic center. These observed dynamics are in agreement with a transition of the enzyme from the ground state into a catalytically competent state. We show that the conformational equilibrium in Xrn2 shifts substantially toward the active state in the presence of substrate and magnesium. Finally, our data reveal that the dynamics in Xrn2 correlate with the RNA degradation rate, as a mutation that attenuates motions also affects catalytic activity. In that light, our results stress the importance of studies that go beyond static structural information.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROMOTES TRANSCRIPTION TERMINATION; SACCHAROMYCES-CEREVISIAE; MESSENGER-RNA; RIBOSOMAL-RNA; ESSENTIAL GENE; DHP1(+) GENE; EXORIBONUCLEASE; RAT1; YEAST; DEGRADATION |
| 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: | 07 Feb 2024 07:05 |
| Last Modified: | 07 Feb 2024 07:05 |
| URI: | https://pred.uni-regensburg.de/id/eprint/56586 |
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