Hierarchical Assembly Pathways of Spermine-Induced Tubulin Conical-Spiral Architectures
| Autor: | Abigail Millgram, Ran Zalk, Israel Ringel, Gabriel A. Frank, Uri Raviv, Raviv Dharan, Asaf Shemesh, Yael Levi-Kalisman |
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| Rok vydání: | 2021 |
| Předmět: |
Polymers
Protein subunit General Physics and Astronomy Spermine macromolecular substances 02 engineering and technology 010402 general chemistry Antiparallel (biochemistry) Microtubules 01 natural sciences chemistry.chemical_compound Tubulin Microtubule General Materials Science Cytoskeleton biology Small-angle X-ray scattering General Engineering 021001 nanoscience & nanotechnology 0104 chemical sciences chemistry ddc:540 biology.protein Biophysics 0210 nano-technology Polyamine |
| Zdroj: | ACS nano 15(5), 8836-8847 (2021). doi:10.1021/acsnano.1c01374 |
| ISSN: | 1936-086X 1936-0851 |
| DOI: | 10.1021/acsnano.1c01374 |
| Popis: | ACS nano 15(5), 8836 - 8847 (2021). doi:10.1021/acsnano.1c01374 Tubulin, an essential cytoskeletal protein, assembles into various morphologies by interacting with an array of cellular factors. One of these factors is the endogenous polyamine spermine, which may promote and stabilize tubulin assemblies. Nevertheless, the assembled structures and their formation pathways are poorly known. Here we show that spermine induced the in vitro assembly of tubulin into several hierarchical architectures based on a tubulin conical-spiral subunit. Using solution X-ray scattering and cryo-TEM, we found that with progressive increase of spermine concentration tubulin dimers assembled into conical-frustum-spirals of increasing length, containing up to three helical turns. The subunits with three helical turns were then assembled into tubules through base-to-top packing and formed antiparallel bundles of tubulin conical-spiral tubules in a distorted hexagonal symmetry. Further increase of the spermine concentration led to inverted tubulin tubules assembled in hexagonal bundles. Time-resolved experiments revealed that tubulin assemblies formed at higher spermine concentrations assembled from intermediates, similar to those formed at low spermine concentrations. These results are distinct from the classical transition between twisted ribbons, helical, and tubular assemblies, and provide insight into the versatile morphologies that tubulin can form. Furthermore, they may contribute to our understanding of the interactions that control the composition and construction of protein-based biomaterials. Published by Soc., Washington, DC |
| Databáze: | OpenAIRE |
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