Modulations of DNA contacts by linker histones and post-translational modifications determine the mobility and modifiability of nucleosomal H3 tails

A Stützer, S Liokatis, A Kiesel, D Schwarzer… - Molecular cell, 2016 - cell.com
Post-translational histone modifications and linker histone incorporation regulate chromatin
structure and genome activity. How these systems interface on a molecular level is unclear …

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

C Vogler, C Huber, T Waldmann, R Ettig, L Braun… - PLoS …, 2010 - journals.plos.org
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 …

Histone core modifications regulating nucleosome structure and dynamics

P Tessarz, T Kouzarides - Nature reviews Molecular cell biology, 2014 - nature.com
Post-translational modifications of histones regulate all DNA-templated processes, including
replication, transcription and repair. These modifications function as platforms for the …

Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription

V Di Cerbo, F Mohn, DP Ryan, E Montellier, S Kacem… - elife, 2014 - elifesciences.org
Post-translational modifications of proteins have emerged as a major mechanism for
regulating gene expression. However, our understanding of how histone modifications …

Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics

M Bernier, Y Luo, KC Nwokelo, M Goodwin… - Nature …, 2015 - nature.com
H1 linker histones are highly abundant proteins that compact nucleosomes and chromatin to
regulate DNA accessibility and transcription. However, the mechanisms that target H1 …

Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure

X Wang, JJ Hayes - Molecular and cellular biology, 2008 - Am Soc Microbiol
Nucleosome arrays undergo salt-dependent self-association into large oligomers in a
process thought to recapitulate essential aspects of higher-order tertiary chromatin structure …

Acetylated histone H4 tail enhances histone H3 tail acetylation by altering their mutual dynamics in the nucleosome

A Furukawa, M Wakamori, Y Arimura… - Proceedings of the …, 2020 - National Acad Sciences
The structural unit of eukaryotic chromatin is a nucleosome, comprising two histone H2A-
H2B heterodimers and one histone (H3-H4) 2 tetramer, wrapped around by∼ 146 bp of …

Histone tail network and modulation in a nucleosome

Y Tsunaka, A Furukawa, Y Nishimura - Current Opinion in Structural …, 2022 - Elsevier
The structural unit of eukaryotic chromatin is a nucleosome, comprising two histone
H2A/H2B heterodimers and one histone (H3/H4) 2 tetramer, wrapped around by∼ 146-bp …

Scratching the (lateral) surface of chromatin regulation by histone modifications

P Tropberger, R Schneider - Nature structural & molecular biology, 2013 - nature.com
Histones have two structurally and functionally distinct domains: globular domains forming
the nucleosomal core around which DNA is wrapped and unstructured tails protruding from …

[HTML][HTML] Clipping of flexible tails of histones H3 and H4 affects the structure and dynamics of the nucleosome

NP Nurse, I Jimenez-Useche, IT Smith, C Yuan - Biophysical journal, 2013 - cell.com
Förster resonance energy transfer was used to monitor the dynamic conformations of
mononucleosomes under different chromatin folding conditions to elucidate the role of the …