Regulation of chromatin structure by site-specific histone H3 methyltransferases

@article{Rea2000RegulationOC,
  title={Regulation of chromatin structure by site-specific histone H3 methyltransferases},
  author={Stephen Rea and Frank Eisenhaber and D I O'Carroll and Brian D. Strahl and Zu-Wen Sun and Manfred Schmid and Susanne Opravil and Karl Mechtler and Chris Paul Ponting and C. David Allis and Thomas Jenuwein},
  journal={Nature},
  year={2000},
  volume={406},
  pages={593-599}
}
The organization of chromatin into higher-order structures influences chromosome function and epigenetic gene regulation. [] Key Result We mapped the catalytic motif to the evolutionarily conserved SET domain, which requires adjacent cysteine-rich regions to confer histone methyltransferase activity. Methylation of lysine 9 interferes with phosphorylation of serine 10, but is also influenced by pre-existing modifications in the amino terminus of H3.

Figures from this paper

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
TLDR
It is shown that mammalian methyltransferases that selectively methylate histone H3 on lysine 9 (Suv39h HMTases) generate a binding site for HP1 proteins—a family of heterochromatic adaptor molecules implicated in both gene silencing and supra-nucleosomal chromatin structure.
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.
The World of SET-Containing Lysine Methyltransferases
TLDR
Methylation of lysines in histones is a post-translational modification regulating gene expression, chromatin remodeling, DNA methylation and non-histone protein function.
Re-SET-ting heterochromatin by histone methyltransferases.
  • T. Jenuwein
  • Biology, Chemistry
    Trends in cell biology
  • 2001
Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
TLDR
The results show that both H3-K9 acetylation and methylation can occur on independent sets of H3 molecules in pericentric heterochromatin, and identify an RNA- and histone modification–dependent structure that brings methylated H1 protein–binding tails together in a specific configuration required for the accumulation of HP1 proteins in these domains.
The many faces of histone lysine methylation.
Arabidopsis Histone Lysine Methyltransferases.
A two-state activation mechanism controls the histone methyltransferase Suv39h1
TLDR
The synthesis of multi-domain ‘designer chromatin’ templates are described and it is proposed that this mechanism serves as a paradigm in chromatin biochemistry since it enables highly dynamic sampling of chromatin state combined with targeted modification of desired genomic regions.
Identification of three histone methyltransferases in Drosophila: dG9a is a suppressor of PEV and is required for gene silencing
TLDR
The identification of three additional Drosophila genes that potentially encode K9H3 specific methyltransferases (HMTase) with homology to known mammalian proteins are described and one of these is a homologue of the human G9a and hence, it is named dG9a.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 55 REFERENCES
Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena.
TLDR
H3 methylation at lysine 4 appears to be specific to macronuclei in Tetrahymena, and it is suggested that this modification pattern plays a facilitatory role in the transcription process in a manner that remains to be determined.
Histone acetylation as an epigenetic determinant of long-term transcriptional competence
  • B. Turner
  • Biology
    Cellular and Molecular Life Sciences CMLS
  • 1998
TLDR
The evidence for the role of acetylation in transcriptional control is outlined, using centric heterochromatin and the dosage-compensated male X chromosome in Drosophila as model systems, and suggests possible mechanisms by which it might operate.
Set Domain-Dependent Regulation of Transcriptional Silencing and Growth Control by SUV39H1, a Mammalian Ortholog ofDrosophila Su(var)3-9
TLDR
A phosphorylation-dependent mechanism for regulating the chromatin organizing activity of a mammalian su(var) protein is suggested and the SET domain is implicate as a gatekeeper motif that integrates upstream signaling pathways to epigenetic regulation and growth control.
Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere
TLDR
Cloned a human cDNA that encodes the 17-kD histone-like centromere antigen, CENP-A, indicates that the assembly of centromeres is driven, at least in part, by the incorporation of a novel core histone into centromeric chromatin.
Structure-Function Analysis of SUV39H1 Reveals a Dominant Role in Heterochromatin Organization, Chromosome Segregation, and Mitotic Progression
TLDR
A dominant role(s) for the SET domain of SUV39H1 in the distribution of prominent heterochromatic proteins is revealed and a possible link between a chromosomal SU(VAR) protein and histone H3 is suggested.
Histone deacetylase homologs regulate epigenetic inheritance of transcriptional silencing and chromosome segregation in fission yeast.
TLDR
The identification of an essential gene, clr6 (cryptic loci regulator), which encodes a putative histone deacetylase that when mutated affects epigenetically maintained repression at the mat2-mat3 region and at centromeres and reduces the fidelity of chromosome segregation is reported.
SET domain proteins modulate chromatin domains in eu- and heterochromatin
TLDR
A model is established in which the modulation of chromatin domains is mechanistically linked with the regulation of key developmental loci (e.g. HOM-C) and multiple functions for chromatin regulators are not restricted to the SET protein family, since many trx-G genes are also modifiers of PEV.
The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast
TLDR
An insertional mutation in Drosophila is identified that enhances PEV and reduces transcription of the gene in the eye–antenna imaginal disc, and corresponds to that encoding the transcriptional regulator RPD3 in yeast and to a human histone deacetylase11.
Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
TLDR
It is proposed that the singular phosphorylation of the amino-terminus of histone H3 may be involved in facilitating two key functions during mitosis: (1) regulate protein-protein interactions to promote binding of trans-acting factors that “drive” chromatin condensation as cells enter M-phase and (2) coordinate chromatin decondensation associated with M- phase.
...
1
2
3
4
5
...