Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

@article{Bannister2001SelectiveRO,
  title={Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain},
  author={Andrew J. Bannister and Philip Zegerman and Janet F. Partridge and Eric Alexander Miska and Jean O. Thomas and Robin C. Allshire and Tony Kouzarides},
  journal={Nature},
  year={2001},
  volume={410},
  pages={120-124}
}
Heterochromatin protein 1 (HP1) is localized at heterochromatin sites where it mediates gene silencing. The chromo domain of HP1 is necessary for both targeting and transcriptional repression. In the fission yeast Schizosaccharomyces pombe, the correct localization of Swi6 (the HP1 equivalent) depends on Clr4, a homologue of the mammalian SUV39H1 histone methylase. Both Clr4 and SUV39H1 methylate specifically lysine 9 of histone H3 (ref. 6). Here we show that HP1 can bind with high affinity to… 

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Specificity of the HP1 chromo domain for the methylated N‐terminus of histone H3
TLDR
In situ immunofluorescence demonstrates that methyl‐K9 H3 and HP1 co‐localize to the heterochromatic regions of Drosophila polytene chromosomes and indicates that sequence diversity in chromo domains may lead to diverse functions in eukaryotic gene regulation.
Speci ® city of the HP 1 chromo domain for the methylated N-terminus of histone
TLDR
In situ immuno ̄uorescence shows that methyl-K9 H3 and HP1 co-localize to the heterochromatic regions of Drosophila polytene chromosomes, and indicates that sequence diversity in chromo domains may lead to diverse functions in eukaryotic gene regulation.
Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains.
TLDR
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.
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.
HP1a Recruitment to Promoters Is Independent of H3K9 Methylation in Drosophila melanogaster
TLDR
It is shown here that Su(var)3-9 controls H3K9me-dependent binding of HP1a in pericentromeric regions, while Setdb1 controls it in cytological region 2L:31 and (together with POF) in chromosome 4.
Rb targets histone H3 methylation and HP1 to promoters
TLDR
It is shown that SUV39H1 and HP1 are both involved in the repressive functions of the retinoblastoma (Rb) protein, and Chromatin immunoprecipitations show that Rb is necessary to direct methylation of histone H3, and is necessary for binding of HP1 to the cyclin E promoter.
SUV39 SET domains mediate crosstalk of heterochromatic histone marks
TLDR
The structure-function approach shows that the H3K14ub substrate binds specifically and tightly to the catalytic domain of Clr4, and thereby stimulates the enzyme by over 250-fold, which mediates licensing of heterochromatin formation.
Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1α
TLDR
It is shown that the association of HP1α with pericentromeric heterochromatin depends not only on its methyl‐binding chromo domain but also on an RNA‐binding activity present in the hinge region of the protein that connects the conserved chromo and chromoshadow domains.
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