Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer
| Autor: | Arunas Silanskas, Edvardas Golovinas, Giedrius Sasnauskas, Mindaugas Zaremba, Danielis Rutkauskas, Marija Jankunec, Elena Manakova |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Molecular biology Science Molecular Conformation Biophysics Piwi-interacting RNA Molecular Dynamics Simulation Cleavage (embryo) Biochemistry Article 03 medical and health sciences chemistry.chemical_compound Structure-Activity Relationship 0302 clinical medicine X-Ray Diffraction RNA interference single molecule Argonaute DNA FRET Scattering Small Angle 030304 developmental biology 0303 health sciences Multidisciplinary 030102 biochemistry & molecular biology Chemistry Archaeoglobus fulgidus Archaea Cell biology Molecular Docking Simulation 030104 developmental biology Förster resonance energy transfer Argonaute Proteins Nucleic acid Medicine Protein Multimerization Structural biology ddc:600 030217 neurology & neurosurgery Function (biology) Protein Binding |
| Zdroj: | Scientific reports, London : Nature, 2021, vol. 11, art. no. 4518, p. 1-14 Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021) Scientific reports 11(1), 4518 (2021). doi:10.1038/s41598-021-83889-4 Scientific Reports |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/s41598-021-83889-4 |
| Popis: | Scientific reports 11(1), 4518 (2021). doi:10.1038/s41598-021-83889-4 Argonaute (Ago) proteins are found in all three domains of life. The best-characterized group is eukaryotic Argonautes (eAgos), which are the core of RNA interference. The best understood prokaryotic Ago (pAgo) proteins are full-length pAgos. They are composed of four major structural/functional domains (N, PAZ, MID, and PIWI) and thereby closely resemble eAgos. It was demonstrated that full-length pAgos function as prokaryotic antiviral systems, with the PIWI domain performing cleavage of invading nucleic acids. However, the majority of identified pAgos are shorter and catalytically inactive (encode just MID and inactive PIWI domains), thus their action mechanism and function remain unknown. In this work we focus on AfAgo, a short pAgo protein encoded by an archaeon Archaeoglobus fulgidus. We find that in all previously solved AfAgo structures, its two monomers form substantial dimerization interfaces involving the C-terminal ��-sheets. Led by this finding, we have employed various biochemical and biophysical assays, including SEC-MALS, SAXS, single-molecule FRET, and AFM, to show that AfAgo is indeed a homodimer in solution, which is capable of simultaneous interaction with two DNA molecules. This finding underscores the diversity of prokaryotic Agos and broadens the range of currently known Argonaute-nucleic acid interaction mechanisms. Published by Macmillan Publishers Limited, part of Springer Nature, [London] |
| Databáze: | OpenAIRE |
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