The Companion of Cellulose Synthase 1 confers salt tolerance through a Tau-like mechanism in plants
| Autor: | Florian Seiter, Ghazanfar Abbas Khan, Edwin R. Lampugnani, Witold G. Szymanski, Arndt Wallmann, René Schneider, Heather E. McFarlane, Clara Sánchez-Rodríguez, Kristina L. Ford, Joshua L. Heazlewood, Christopher Kesten, Peter Schmieder, Barth-Jan van Rossum, Hartmut Oschkinat, Anne Diehl, Staffan Persson, Nils Cremer |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Cell division Microtubule-associated protein Science Tau protein Arabidopsis General Physics and Astronomy tau Proteins 02 engineering and technology Microtubules Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Microtubule lcsh:Science Cellulose Multidisciplinary biology ATP synthase Arabidopsis Proteins Chemistry Salt Tolerance General Chemistry 021001 nanoscience & nanotechnology Plant cell biology.organism_classification 030104 developmental biology Tubulin Glucosyltransferases Seedlings Biophysics biology.protein lcsh:Q 0210 nano-technology Hydrophobic and Hydrophilic Interactions Microtubule-Associated Proteins |
| Zdroj: | Nature Communications, 10 (1) Nature Communications Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019) |
| ISSN: | 2041-1723 |
| Popis: | Microtubules arefilamentous structures necessary for cell division, motility and morphology,with dynamics critically regulated by microtubule-associated proteins (MAPs). Here weoutline the molecular mechanism by which the MAP, COMPANION OF CELLULOSE SYN-THASE1 (CC1), controls microtubule bundling and dynamics to sustain plant growth undersalt stress. CC1 contains an intrinsically disordered N-terminus that links microtubules atevenly distributed points through four conserved hydrophobic regions. By NMR and live cellanalyses we reveal that two neighboring residues in thefirst hydrophobic binding motif arecrucial for the microtubule interaction. The microtubule-binding mechanism of CC1 isreminiscent to that of the prominent neuropathology-related protein Tau, indicating evolu-tionary convergence of MAP functions across animal and plant cells. Nature Communications, 10 (1) ISSN:2041-1723 |
| Databáze: | OpenAIRE |
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