PuSH - Publication Server of Helmholtz Zentrum München

Vogler, C.* ; Huber, C.* ; Waldmann, T.* ; Ettig, R.* ; Braun, L.* ; Izzo, A.* ; Daujat, S.* ; Chassignet, I.* ; Lopez-Contreras, A.J.* ; Fernandez-Capetillo, O.* ; Dundr, M.* ; Rippe, K.* ; Längst, G.* ; Schneider, R.*

Histone H2A C-terminus regulates chromatin dynamics, remodeling, and histone H1 binding.

PLoS Genet. 6:e1001234 (2010)
DOI PMC
Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
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.
Altmetric
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
ISSN (print) / ISBN 1553-7390
e-ISSN 1553-7404
Journal PLoS Genetics
Quellenangaben Volume: 6, Issue: 12, Pages: , Article Number: e1001234 Supplement: ,
Publisher Public Library of Science (PLoS)
Non-patent literature Publications
Reviewing status Peer reviewed