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Illuminating the Reaction Pathways of Viromimetic Assembly
[Image: see text] The coassembly of well-defined biological nanostructures relies on a delicate balance between attractive and repulsive interactions between biomolecular building blocks. Viral capsids are a prototypical example, where coat proteins exhibit not only self-interactions but also intera...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5388896/ https://www.ncbi.nlm.nih.gov/pubmed/28326772 http://dx.doi.org/10.1021/jacs.7b01401 |
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author | Cingil, Hande E. Boz, Emre B. Biondaro, Giovanni de Vries, Renko Cohen Stuart, Martien A. Kraft, Daniela J. van der Schoot, Paul Sprakel, Joris |
author_facet | Cingil, Hande E. Boz, Emre B. Biondaro, Giovanni de Vries, Renko Cohen Stuart, Martien A. Kraft, Daniela J. van der Schoot, Paul Sprakel, Joris |
author_sort | Cingil, Hande E. |
collection | PubMed |
description | [Image: see text] The coassembly of well-defined biological nanostructures relies on a delicate balance between attractive and repulsive interactions between biomolecular building blocks. Viral capsids are a prototypical example, where coat proteins exhibit not only self-interactions but also interact with the cargo they encapsulate. In nature, the balance between antagonistic and synergistic interactions has evolved to avoid kinetic trapping and polymorphism. To date, it has remained a major challenge to experimentally disentangle the complex kinetic reaction pathways that underlie successful coassembly of biomolecular building blocks in a noninvasive approach with high temporal resolution. Here we show how macromolecular force sensors, acting as a genome proxy, allow us to probe the pathways through which a viromimetic protein forms capsids. We uncover the complex multistage process of capsid assembly, which involves recruitment and complexation, followed by allosteric growth of the proteinaceous coat. Under certain conditions, the single-genome particles condense into capsids containing multiple copies of the template. Finally, we derive a theoretical model that quantitatively describes the kinetics of recruitment and growth. These results shed new light on the origins of the pathway complexity in biomolecular coassembly. |
format | Online Article Text |
id | pubmed-5388896 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-53888962017-04-13 Illuminating the Reaction Pathways of Viromimetic Assembly Cingil, Hande E. Boz, Emre B. Biondaro, Giovanni de Vries, Renko Cohen Stuart, Martien A. Kraft, Daniela J. van der Schoot, Paul Sprakel, Joris J Am Chem Soc [Image: see text] The coassembly of well-defined biological nanostructures relies on a delicate balance between attractive and repulsive interactions between biomolecular building blocks. Viral capsids are a prototypical example, where coat proteins exhibit not only self-interactions but also interact with the cargo they encapsulate. In nature, the balance between antagonistic and synergistic interactions has evolved to avoid kinetic trapping and polymorphism. To date, it has remained a major challenge to experimentally disentangle the complex kinetic reaction pathways that underlie successful coassembly of biomolecular building blocks in a noninvasive approach with high temporal resolution. Here we show how macromolecular force sensors, acting as a genome proxy, allow us to probe the pathways through which a viromimetic protein forms capsids. We uncover the complex multistage process of capsid assembly, which involves recruitment and complexation, followed by allosteric growth of the proteinaceous coat. Under certain conditions, the single-genome particles condense into capsids containing multiple copies of the template. Finally, we derive a theoretical model that quantitatively describes the kinetics of recruitment and growth. These results shed new light on the origins of the pathway complexity in biomolecular coassembly. American Chemical Society 2017-03-22 2017-04-05 /pmc/articles/PMC5388896/ /pubmed/28326772 http://dx.doi.org/10.1021/jacs.7b01401 Text en Copyright © 2017 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes. |
spellingShingle | Cingil, Hande E. Boz, Emre B. Biondaro, Giovanni de Vries, Renko Cohen Stuart, Martien A. Kraft, Daniela J. van der Schoot, Paul Sprakel, Joris Illuminating the Reaction Pathways of Viromimetic Assembly |
title | Illuminating
the Reaction Pathways of Viromimetic
Assembly |
title_full | Illuminating
the Reaction Pathways of Viromimetic
Assembly |
title_fullStr | Illuminating
the Reaction Pathways of Viromimetic
Assembly |
title_full_unstemmed | Illuminating
the Reaction Pathways of Viromimetic
Assembly |
title_short | Illuminating
the Reaction Pathways of Viromimetic
Assembly |
title_sort | illuminating
the reaction pathways of viromimetic
assembly |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5388896/ https://www.ncbi.nlm.nih.gov/pubmed/28326772 http://dx.doi.org/10.1021/jacs.7b01401 |
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