Structural dynamics govern substrate recruitment and catalytic turnover in H/ACA RNP pseudouridylation
| Autor: | Gerd Hanspach, Andreas U. Schmidt, Martin Hengesbach |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Fluorophore
Archaeal Proteins Protein domain Biology Catalysis 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Ribonucleoproteins Small Nucleolar RNA Small Nucleolar Guide RNA Molecular Biology Base Pairing 030304 developmental biology Ribonucleoprotein 0303 health sciences Mutagenesis Cell Biology Ribosomal RNA Pyrococcus furiosus Förster resonance energy transfer chemistry 030220 oncology & carcinogenesis Biophysics Spliceosomes Function (biology) Pseudouridine RNA Guide Kinetoplastida Research Paper |
| Zdroj: | RNA Biol |
| ISSN: | 1555-8584 |
| Popis: | H/ACA ribonucleoproteins catalyse the sequence-dependent pseudouridylation of ribosomal and spliceosomal RNAs. Here, we reconstitute site-specifically fluorophore labelled H/ACA complexes and analyse their structural dynamics using single-molecule FRET spectroscopy. Our results show that the guide RNA is distorted into a substrate-binding competent conformation by specific protein interactions. Analysis of the reaction pathway using atomic mutagenesis establishes a new model how individual protein domains contribute to catalysis. Taken together, these results identify and characterize individual roles for all accessory proteins on the assembly and function of H/ACA RNPs. |
| Databáze: | OpenAIRE |
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