| Autor: |
Laura Maguire, Kaushik Dutta, Michael P. Rout, Deniz B. Temel, Alia Kamal, Kathryn P. Wall, Jaclyn Tetenbaum-Novatt, Geoff Armstrong, Loren E. Hough, Samuel Sparks, David Cowburn |
| Rok vydání: |
2016 |
| Předmět: |
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| Zdroj: |
Biophysical Journal. 110(3) |
| ISSN: |
0006-3495 |
| DOI: |
10.1016/j.bpj.2015.11.2983 |
| Popis: |
Nuclear pore complexes form a selective filter that allows the rapid passage of transport factors and their cargoes across the nuclear envelope, while blocking the passage of other macromolecules. Intrinsically disordered proteins (IDPs) containing phenylalanyl-glycyl (FG) rich repeats line the pore and interact with transport factors. However, the reason that transport can be both fast and specific remains undetermined, through lack of atomic-scale information on the behavior of FGs and their interaction with transport factors. We report on recently published (Hough et. al. eLife 2015) as well as subsequent experiments to probe the molecular mechanism of transport. We used biophysical characterization and nuclear magnetic resonance both in solution and within the bacterial and yeast cellular environments to probe the molecular mechanism of transport and the role of disorder in this process. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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