| Autor: |
Guidotti N; Laboratory of Biophysical Chemistry of Macromolecules, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland. beat.fierz@epfl.ch., Lechner CC, Fierz B |
| Jazyk: |
angličtina |
| Zdroj: |
Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2017 Sep 14; Vol. 53 (74), pp. 10267-10270. |
| DOI: |
10.1039/c7cc06180c |
| Abstrakt: |
In stem cells, H4 proteins carrying different modifications coexist within single nucleosomes. For functional studies, we report the synthesis of such asymmetric nucleosomes. Asymmetry is achieved by transiently crosslinking H4 by a traceless, protease-removable tag introduced via an isopeptide linkage. These nucleosomes are used to study Set8 activity, a key methyltransferase. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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