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The language of covalent histone modifications
It is proposed that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.
Translating the Histone Code
It is proposed that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.
Regulation of chromatin structure by site-specific histone H3 methyltransferases
A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex.
The function of Gcn5 as a hist one acetyltransferase within the Ada and SAGA adaptor complexes indicates the importance of histone acetylation during steps in transcription activation mediated by interactions with transcription activators and general transcription factors.
Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly
In vivo evidence is provided that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast, defining a conserved pathway wherein sequential histone modifications establish a “histone code” essential for the epigenetic inheritance of heterochROMatin assembly.
This review discusses the current understanding of histone acetyl transferases (HATs) or acetyltransferases (ATs): their discovery, substrate specificity, catalytic mechanism, regulation, and functional links to transcription, as well as to other chromatin-modifying activities.
Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
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.
Regulation of HP1–chromatin binding by histone H3 methylation and phosphorylation
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.
DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA
DNMT3L recognizes histone H3 tails that are unmethylated at lysine 4 and induces de novo DNA methylation by recruitment or activation of DNMT3A2, and substitution of key residues in the binding site eliminated the H3 tail–DN MT3L interaction.
Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains.
- W. Fischle, Yanming Wang, S. Jacobs, Youngchang Kim, C. Allis, S. Khorasanizadeh
- Biology, ChemistryGenes & development
- 1 August 2003
It is shown that the chromodomain proteins Polycomb (Pc) and HP1 (heterochromatin protein 1) are highly discriminatory for binding to these sites in vivo and in vitro, and a role for their Chromodomains in both target site binding and discrimination is indicated.