Unknown

Dataset Information

0

Dynamic interplay between histone H3 modifications and protein interpreters: emerging evidence for a "histone language".


ABSTRACT: Histone proteins organize DNA into dynamic chromatin structures and regulate processes such as transcription, repair, and replication. Control of chromatin function and structure is mediated in part by reversible post-translational modifications (PTMs) on histones. The most N-terminal region of histone H3 contains a high density of modifiable residues. Here we focus on the dynamic interplay between histone modification states on the H3 N terminus and the binding modules that recognize these states. Specifically, we discuss the effect of auxiliary modifications to H3K4unmod/me3 binding modules (specifically H3R2 methylation, H3T3 phosphorylation, and H3T6 phosphorylation). Emerging evidence suggests that histone PTMs behave less like a strict "code", but more like a "language", which better illustrates the importance of context. Using androgen-receptor-mediated gene activation as an example, we propose a model of how the combinatorial natures of PTMs on the H3 N terminus and the complexes that recognize these epigenetic modifications control gene expression.

SUBMITTER: Oliver SS 

PROVIDER: S-EPMC3073147 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Dynamic interplay between histone H3 modifications and protein interpreters: emerging evidence for a "histone language".

Oliver Samuel S SS   Denu John M JM  

Chembiochem : a European journal of chemical biology 20101029 2


Histone proteins organize DNA into dynamic chromatin structures and regulate processes such as transcription, repair, and replication. Control of chromatin function and structure is mediated in part by reversible post-translational modifications (PTMs) on histones. The most N-terminal region of histone H3 contains a high density of modifiable residues. Here we focus on the dynamic interplay between histone modification states on the H3 N terminus and the binding modules that recognize these stat  ...[more]

Similar Datasets

| S-EPMC8047140 | biostudies-literature
| S-EPMC4099280 | biostudies-literature
| S-EPMC4417181 | biostudies-literature
| S-EPMC3302642 | biostudies-literature
| S-EPMC9271290 | biostudies-literature
| S-EPMC4423362 | biostudies-literature
| S-EPMC4580250 | biostudies-literature
| S-EPMC4099259 | biostudies-literature
2023-10-19 | PXD039495 | Pride
| S-EPMC7020651 | biostudies-literature