Structural insights into filament recognition by cellular actin markers
| Autor: | Kutti R. Vinothkumar, Archana Kumari, Minhajuddin Sirajuddin, Shubham Kesarwani, Manjunath G Javoor |
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| Rok vydání: | 2019 |
| Předmět: |
0303 health sciences
biology Cryo-electron microscopy Phalloidin macromolecular substances Computational biology Filamentous actin Protein filament 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine chemistry Utrophin biology.protein Actin-binding protein Binding site 030217 neurology & neurosurgery Actin 030304 developmental biology |
| DOI: | 10.1101/846337 |
| Popis: | Cellular studies of filamentous actin (F-actin) processes commonly utilize fluorescent versions of toxins, peptides and proteins that bind actin. While the choice of these markers has been largely based on availability and ease, there is a severe dearth of structural data for an informed judgment in employing suitable F-actin markers for a particular requirement. Here we describe the electron cryomicroscopy structures of phalloidin, lifeAct and utrophin bound to F-actin, providing the first high-resolution structures and comparison of widely used actin markers and their influence towards F-actin. Our results show that phalloidin binding does not induce conformations and lifeAct specifically recognizes ADP-actin state, which can be used as a sensor for distinguishing different nucleotide states of F-actin. The utrophin structural model aided designing minimal utrophin, which can be utilized as F-actin marker. Together, our study provides a structural perspective, where the binding sites of utrophin and lifeAct overlap with majority of actin binding proteins. Further offering an invaluable resource for researchers in choosing appropriate actin markers and generating new marker variants. |
| Databáze: | OpenAIRE |
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