Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

@article{Lachner2001MethylationOH,
  title={Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins},
  author={Monika Lachner and D{\'o}nal O’Carroll and Stephen Rea and Karl Mechtler and Thomas Jenuwein},
  journal={Nature},
  year={2001},
  volume={410},
  pages={116-120}
}
Distinct modifications of histone amino termini, such as acetylation, phosphorylation and methylation, have been proposed to underlie a chromatin-based regulatory mechanism that modulates the accessibility of genetic information. In addition to histone modifications that facilitate gene activity, it is of similar importance to restrict inappropriate gene expression if cellular and developmental programmes are to proceed unperturbed. Here we show that mammalian methyltransferases that… 
Regulation of HP1–chromatin binding by histone H3 methylation and phosphorylation
TLDR
It is shown that HP1α, -β, and -γ are released from chromatin during the M phase of the cell cycle, even though tri-methylation levels of histone H3 lysine 9 remain unchanged, and a regulatory mechanism of protein–protein interactions is established through a combinatorial readout of two adjacent post-translational modifications: a stable methylation and a dynamic phosphorylation mark.
Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin
TLDR
It is shown that H3–Lys9 methylation is retained through mitosis, indicating that it might provide an epigenetic imprint for the maintenance of the inactive state, and suggest the existence of an Suv39h-HP1-independent pathway regulating H3-Lys 9 methylation of facultative heterochromatin.
HP1 Binding to Chromatin Methylated at H3K9 Is Enhanced by Auxiliary Factors
TLDR
It is proposed that HP1 has multiple target sites that contribute to its recognition of chromatin, only one of them being methylated at H3K9, which has implications for the mechanisms of recognition of specific chromatin modifications in vivo.
Balance between Acetylation and Methylation of Histone H3 Lysine 9 on the E2F-Responsive Dihydrofolate Reductase Promoter
TLDR
The results indicate that the temporal regulation of euchromatic promoters may involve controlling the balance between methylation and acetylation of histone H3 lysine 9, a feature previously described for the spatial regulation of chromatin function.
Dynamic Regulation of Effector Protein Binding to Histone Modifications: The Biology of HP1 Switching
TLDR
The biological function of HP1 release from chromatin during mitosis is discussed, implications why the cell controls HP1 binding by such a methylation-phosphorylation switching mechanism are considered, and reflect on other cellular pathways where binary switching ofHP1 might occur.
Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
TLDR
It is shown that antibodies against mitotic chromosomal antigens that are associated with human autoimmune diseases specifically recognize H3 molecules that are modified by both tri-methylation of lysine’9 and phosphorylation of serine 10 (H3K9me3S10ph).
The many faces of histone lysine methylation.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 30 REFERENCES
Regulation of chromatin structure by site-specific histone H3 methyltransferases
TLDR
A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
Histone acetylation and an epigenetic code.
  • B. Turner
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 2000
TLDR
Recent evidence raises the interesting possibility that an acetylation-based code may operate through both mitosis and meiosis, providing a possible mechanism for germ-line transmission of epigenetic changes.
Heterochromatin protein 1 binds to nucleosomes and DNA in vitro.
TLDR
It is shown that histone H4 amino-terminal peptides bind to monomeric and dimeric HP1 in vitro, suggesting that HP1 may serve as a cross-linker in chromatin, linking nucleosomal DNA and nonhistone protein complexes to form higher order chromatin structures.
Functional analysis of the chromo domain of HP1.
TLDR
It is reported here that point mutations in the HP1 chromo domain abolish the ability of HP1 to promote gene silencing, supporting the view that the chromodomain homology reflects a common mechanistic basis for homeotic and heterochromatic silencing.
The Drosophila Polycomb Protein Interacts with Nucleosomal Core Particles In Vitro via Its Repression Domain
TLDR
The results suggest that PC, by binding to the core particle, recruits other PcG proteins to chromatin, which could provide a key step in the establishment or regulation of higher-order chromatin structures.
Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family
TLDR
An association of TIF1β with both heterochromatin and euchromatin in interphase nuclei is reported and it is shown that trichostatin A, an inhibitor of histone deacetylases, can interfere with both Tif1 and HP1 silencing.
Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells
TLDR
Biochemical analysis showed that HP1α and HP1γ are phosphorylated throughout the cell cycle, although more extensively in mitosis than in interphase, while HP1β apparently remains unphosphorylated.
KAP-1 Corepressor Protein Interacts and Colocalizes with Heterochromatic and Euchromatic HP1 Proteins: a Potential Role for Krüppel-Associated Box–Zinc Finger Proteins in Heterochromatin-Mediated Gene Silencing
TLDR
A mechanism for the recruitment of HP1-like gene products by the KRAB-ZFP–KAP-1 complex to specific loci within the genome through formation of heterochromatin-like complexes that silence gene activity is suggested.
...
1
2
3
...