Methylation of Lysine 9 in Histone H3 Directs Alternative Modes of Highly Dynamic Interaction of Heterochromatin Protein hHP1β with the Nucleosome

Munari, Francesca; Soeroes, Szabolcs; Zenn, Hans Michael; Schomburg, Adrian; Kost, Nils; Schröder, Sabrina; Klingberg, Rebecca; Rezaei‐Ghaleh, Nasrollah; Stützer, Alexandra; Gelato, Kathy A.; Walla, Peter Jomo; Becker, Stefan; Schwarzer, Dirk; Zimmermann, Bastian; Fischle, Wolfgang; Zweckstetter, Markus

doi:10.1074/jbc.m112.390849

Cited by 60 publications

(91 citation statements)

References 50 publications

(74 reference statements)

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“…The discovery that the HP1 CD binds histone H3K9Me2/3 led to models in which this interaction provides the structural basis for the condensed structure of pericentric heterochromatin (5)(6)(7)44). Despite studies showing that histone H3K9Me3 methylation in nucleosomal arrays facilitates HP1 binding (15,16), details regarding the nature of the complex and the consequences of binding remained unknown.…”

Section: Discussionmentioning

confidence: 99%

Human Heterochromatin Protein 1α Promotes Nucleosome Associations That Drive Chromatin Condensation

Azzaz

Vitalini

Thomas

et al. 2014

Journal of Biological Chemistry

102

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Background:Heterochromatin is enriched for di-and tri-methylated lysine 9 of histone H3 (H3K9Me2/3) and heterochromatin protein 1 (HP1 Hs␣ . ). Results: The association of HP1Hs␣ with H3K9Me3-containing nucleosome arrays facilitated array compaction and cross-array interactions. Conclusion: HP1Hs␣ association caused intra-and inter-array associations, leading to chromatin condensation and looping. Significance: An understanding of HP1Hs␣ -nucleosome interactions provides insights on the structure and functions of heterochromatin.

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Section: Discussionmentioning

confidence: 99%

Human Heterochromatin Protein 1α Promotes Nucleosome Associations That Drive Chromatin Condensation

Azzaz

Vitalini

Thomas

et al. 2014

Journal of Biological Chemistry

102

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“…In addition, even if HP1 was not identified as one of the main nodes, it has been studied in this research because H3K9me3 is directly linked to HP1. This link may be biologically explained because H3K9me3 serves as a binding platform for HP1 recruitment (Bannister et al 2001;Lachner et al 2001;Munari et al 2012). Analogously, HP1 in turn recruits Dnmts along with a multiprotein complex that also includes G9a and SUV39H1 (Estève et al 2006;Smallwood et al 2007), thus contributing to define an inactive condensed chromatin configuration.…”

Section: Discussionmentioning

confidence: 99%

H3K9 Trimethylation Precedes DNA Methylation during Sheep Oogenesis

Russo

Bernabò

Giacinto

et al. 2012

J Histochem Cytochem.

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SummaryThe oocyte, to become a fully mature gamete, has to acquire a correct pattern of DNA methylation on its genome; this epigenetic event represents the major point of the molecular mechanisms that occur during postnatal oogenesis. It is known that an intimate link exists between DNA methylation and histone posttranslational modifications, such as trimethylation of lysine 9 on histone 3 (H3K9me3), that is essential in the silencing of gene transcription. What remains unclear is the precise sequence of these two epigenetic events and the protein expression of the enzymes that catalyze this epigenetic maturation during oogenesis. To identify the key molecules involved in global DNA methylation and H3K9me3, a biological network-based computational model was realized. Then, the spatiotemporal distribution of the proteins, identified from the biological network, was assessed during postnatal oogenesis. The results obtained suggest the existence of a sequential cascade of events in which H3K9me3 is the primary step followed by DNA methylation. These two epigenetic marks are realized due to the recruitment of the HDAC1, SUV39H1, G9a, HP1, and Dnmt3a, which were always localized in the nuclei of the oocytes and were dependent on chromatin configuration. These results involving DNA methylation and H3K9me3 are crucial in defining the oocyte developmental competence. (J Histochem Cytochem 61:75-89, 2013)

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“…Nucleosomes contained a 187-bp-long DNA fragment with the 601 DNA sequence at its center (Munari et al, 2012). The histone mutant H3S28A was generated by site-directed mutagenesis.…”

Section: Scanning Electron Microscopymentioning

confidence: 99%

Histone H3 Serine 28 Is Essential for Efficient Polycomb-Mediated Gene Repression in Drosophila

et al. 2015

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Trimethylation at histone H3K27 is central to the polycomb repression system. Juxtaposed to H3K27 is a widely conserved phosphorylatable serine residue (H3S28) whose function is unclear. To assess the importance of H3S28, we generated a Drosophila H3 histone mutant with a serine-to-alanine mutation at position 28. H3S28A mutant cells lack H3S28ph on mitotic chromosomes but support normal mitosis. Strikingly, all methylation states of H3K27 drop in H3S28A cells, leading to Hox gene derepression and to homeotic transformations in adult tissues. These defects are not caused by active H3K27 demethylation nor by the loss of H3S28ph. Biochemical assays show that H3S28A nucleosomes are a suboptimal substrate for PRC2, suggesting that the unphosphorylated state of serine 28 is important for assisting in the function of polycomb complexes. Collectively, our data indicate that the conserved H3S28 residue in metazoans has a role in supporting PRC2 catalysis.

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Methylation of Lysine 9 in Histone H3 Directs Alternative Modes of Highly Dynamic Interaction of Heterochromatin Protein hHP1β with the Nucleosome

Cited by 60 publications

References 50 publications

Human Heterochromatin Protein 1α Promotes Nucleosome Associations That Drive Chromatin Condensation

Human Heterochromatin Protein 1α Promotes Nucleosome Associations That Drive Chromatin Condensation

H3K9 Trimethylation Precedes DNA Methylation during Sheep Oogenesis

Histone H3 Serine 28 Is Essential for Efficient Polycomb-Mediated Gene Repression in Drosophila

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