The language of covalent histone modifications

@article{Strahl2000TheLO,
  title={The language of covalent histone modifications},
  author={Brian D. Strahl and C. David Allis},
  journal={Nature},
  year={2000},
  volume={403},
  pages={41-45}
}
Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose that distinct histone modifications, on one or more tails… Expand
Regulated nucleosome mobility and the histone code
TLDR
A new and testable model for how cells implement the histone code by modulating nucleosome dynamics is proposed. Expand
Alterations of Histone Modifications in Cancer
TLDR
It is well documented that the post-translational modifications of both histone tails and the histone core domain have a critical role in chromatin organization and consequently in the cellular processes correlated with them, such as gene transcription, DNA replication, condensation, and repair. Expand
Connecting the DOTs: covalent histone modifications and the formation of silent chromatin.
TLDR
A flurry of recent papers now describe a third class of HMT that affects chromatin silencing indirectly, not by methylation of histone tails, but instead by targeting a conserved lysine residue in the core domain of the nucleosome. Expand
Reading signals on the nucleosome with a new nomenclature for modified histones
  • B. Turner
  • Biology, Medicine
  • Nature Structural &Molecular Biology
  • 2005
TLDR
A nomenclature is presented that allows patterns of histone modification to be clearly and unambiguously specified and that should facilitate discussion of their functional roles. Expand
Protein modules that manipulate histone tails for chromatin regulation
  • R. Marmorstein
  • Biology, Medicine
  • Nature Reviews Molecular Cell Biology
  • 2001
TLDR
It is becoming clear that appropriate coordination of histone modifications and their manipulations by conserved protein modules are integral to gene-specific transcriptional regulation within chromatin. Expand
How does the histone code work?
TLDR
Findings that the structured globular domain of the nucleosome core particle plays a key role regulating chromatin dynamics are reviewed and calls for the re-examination of current models for the epigenetic regulation of chromatin structure. Expand
How does the histone code work ? 1
Patterns of histone post-translational modifications correlate with distinct chromosomal states that regulate access to DNA, leading to the histone-code hypothesis. However, it is not clear howExpand
The Histone Modification Circus
TLDR
New results are discussed that elucidate the sequence of reactions that modify histone H3 and how these modifications translate into gene silencing in fission yeast. Expand
Combinatorial complexity in chromatin structure and function: revisiting the histone code.
  • O. Rando
  • Biology, Medicine
  • Current opinion in genetics & development
  • 2012
TLDR
This review will focus on contrasting results of functional and localization studies finding minimal combinatorial complexity in histone modification patterns, and possible ways to reconcile these conflicting views. Expand
The modification and variants of histone
TLDR
Recent progress in understanding how histone variants lead to changes in chromatin structure and dynamics to carry out specific functions is discussed. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 78 REFERENCES
The histone tails of the nucleosome.
TLDR
The high-resolution X-ray structure of the nucleosome core particle, as well as earlier evidence, suggests that the histone tails are largely responsible for the assembly of nucleosomes into chromatin fibers and implies that the physiological effects of histone acetylation may be achieved by modulation of a dynamic inter-conversion between the fiber and a less condensed nucleofilament structure. Expand
Histone acetylation in chromatin and chromosomes.
TLDR
New approaches allowing exploration of the molecular details, the functional effects and the regulation of histone acetylation promise to reveal new mechanisms of genomic regulation. Expand
How do histone acetyltransferases select lysine residues in core histones?
TLDR
A putative rule for lysine selection by HATs is proposed based on the primary sequence in the vicinity of lysines in the core histone N‐terminal tails and in flanking sequence to provide insight into the molecular basis of site selection of core histones by H ATs. Expand
Patterns of histone acetylation.
TLDR
Study of the specificity of site utilisation in the monoacetyl, diacetyl and triacetyl forms of histones H3, H4 and H2B reinforces the view that lysine acetylation in core histones is a very specific phenomenon that plays several functionally distinct roles. Expand
Structure and function of the core histone N-termini: more than meets the eye.
TLDR
Evidence supporting the new concepts that when functioning in their natural chromatin context, the N-termini are engaged primarily in protein-protein interactions is discussed, and the global structure and function of any given region of the genome will be determined predominantly by the core histone N- termini and their specific interaction partners. Expand
Histone acetylation in chromatin structure and transcription
TLDR
The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle, which may direct histone assembly and help regulate the unfolding and activity of genes. Expand
Chromatin disruption and modification.
TLDR
The possible structural basis and functional consequences of the observed alterations in chromatin associated with transcriptional activation and repression are discussed. Expand
Gene activation by histone and factor acetyltransferases.
  • S. Berger
  • Biology, Medicine
  • Current opinion in cell biology
  • 1999
TLDR
The first atomic resolution structures of HATs have revealed conserved mechanisms of acetyl-CoA interaction among the superfamily of GNATs (Gcn5-related N-acetyltransferases), and enzymatic acetyltransferase activities are themselves regulated by phosphorylation and interaction with other proteins. Expand
Histone deacetylase
TLDR
According to this model, the rapid deacetylation of distinct lysines in especially H2A and H2B would facilitate the association of anionic protein domains of regulatory proteins to specific nucleosomes and may represent a unique regulatory mechanism in the early steps of gene activation. Expand
Role of histone tails in nucleosome remodeling by Drosophila NURF
TLDR
It is shown that the interaction between NURF and nucleosomes is impaired by proteolytic removal of the N‐terminal histone tails and by chemical cross‐linking of nucleosomal histones, and this role may, in part, be independent of histone acetylation. Expand
...
1
2
3
4
5
...