TY - JOUR

T1 - Histone H2A C-terminus regulates chromatin dynamics, remodeling, and histone H1 binding

AU - Vogler, Christine

AU - Huber, Claudia

AU - Waldmann, Tanja

AU - Ettig, Ramona

AU - Braun, Lora

AU - Izzo, Annalisa

AU - Daujat, Sylvain

AU - Chassignet, Isabelle

AU - Lopez-Contreras, Andres Joaquin

AU - Fernandez-Capetillo, Oscar

AU - Dundr, Miroslav

AU - Rippe, Karsten

AU - Längst, Gernot

AU - Schneider, Robert

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

KW - Amino Acid Motifs

KW - Cell Line

KW - Chromatin

KW - Chromatin Assembly and Disassembly

KW - Histones

KW - Humans

KW - Nucleosomes

KW - Protein Binding

U2 - 10.1371/journal.pgen.1001234

DO - 10.1371/journal.pgen.1001234

M3 - Journal article

C2 - 21170357

VL - 6

SP - e1001234

JO - P L o S Genetics

JF - P L o S Genetics

SN - 1553-7390

IS - 12

ER -