Vogler, Christine and Huber, Claudia and Waldmann, Tanja and Ettig, Ramona and Braun, Lora and Izzo, Annalisa and Daujat, Sylvain and Chassignet, Isabelle and Joaquin Lopez-Contreras, Andres and Fernandez-Capetillo, Oscar and Dundr, Miroslav and Rippe, Karsten and Laengst, Gernot and Schneider, Robert (2010) Histone H2A C-Terminus Regulates Chromatin Dynamics, Remodeling, and Histone H1 Binding. PLOS GENETICS, 6 (12): e1001234. ISSN 1553-7404,
Full text not available from this repository. (Request a copy)Abstract
The tails of histone proteins are central players for all chromatin-mediated processes. Whereas the N-terminal histone tails have been studied extensively, little is known about the function of the H2A C-terminus. Here, we show that the H2A C-terminal tail plays a pivotal role in regulating chromatin structure and dynamics. We find that cells expressing C-terminally truncated H2A show increased stress sensitivity. Moreover, both the complete and the partial deletion of the tail result in increased histone exchange kinetics and nucleosome mobility in vivo and in vitro. Importantly, our experiments reveal that the H2A C-terminus is required for efficient nucleosome translocation by ISWI-type chromatin remodelers and acts as a novel recognition module for linker histone H1. Thus, we suggest that the H2A C-terminal tail has a bipartite function: stabilisation of the nucleosomal core particle, as well as mediation of the protein interactions that control chromatin dynamics and conformation.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NUCLEOSOME CORE PARTICLE; LINKER HISTONE; IN-VIVO; SACCHAROMYCES-CEREVISIAE; ANGSTROM RESOLUTION; MOLECULAR-DYNAMICS; DNA; CELLS; MOBILIZATION; OCTAMER; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III > Prof. Dr. Gernot Längst |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 07 Jul 2020 04:51 |
| Last Modified: | 07 Jul 2020 04:51 |
| URI: | https://pred.uni-regensburg.de/id/eprint/23833 |
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