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Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE260722 | GEO | 2025/07/30

REPOSITORIES: GEO

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Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation [CUT&Run_2]

Project description:We profiled H4K20 monomethylation and KMT5A during the well-characterized erythroid differentiation of human hematopoietic stem and progenitor cells.

2025-07-30 | GSE300158 | GEO

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&Tag)

Project description:We profiled H4K20 mono- and tri- methylation during the well-characterized erythroid differentiation of human hematopoietic stem and progenitor cells.

2025-07-30 | GSE260721 | GEO

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&RUN)

Project description:We profiled H4K20 mono- and tri- methylation during the well-characterized erythroid differentiation of human hematopoietic stem and progenitor cells.

2025-07-30 | GSE260720 | GEO

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation

Project description:Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation

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Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&Tag)

Project description:Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&Tag)

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Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&RUN)

Project description:Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&RUN)

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Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation [CUT&Run_2]

Project description:Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation [CUT&Run_2]

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Structural basis of nucleosomal histone H4 lysine 20 methylation by SET8 methyltransferase.

Project description:SET8 is solely responsible for histone H4 lysine-20 (H4K20) monomethylation, which preferentially occurs in nucleosomal H4. However, the underlying mechanism by which SET8 specifically promotes the H4K20 monomethylation in the nucleosome has not been elucidated. Here, we report the cryo-EM structures of the human SET8-nucleosome complexes with histone H3 and the centromeric H3 variant, CENP-A. Surprisingly, we found that the overall cryo-EM structures of the SET8-nucleosome complexes are substantially different from the previous crystal structure models. In the complexes with H3 and CENP-A nucleosomes, SET8 specifically binds the nucleosomal acidic patch via an arginine anchor, composed of the Arg188 and Arg192 residues. Mutational analyses revealed that the interaction between the SET8 arginine anchor and the nucleosomal acidic patch plays an essential role in the H4K20 monomethylation activity. These results provide the groundwork for understanding the mechanism by which SET8 specifically accomplishes the H4K20 monomethylation in the nucleosome.

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Preferential dimethylation of histone H4 lysine 20 by Suv4-20.

Project description:Post-translational modifications of histone tails direct nuclear processes including transcription, DNA repair, and chromatin packaging. Lysine 20 of histone H4 is mono-, di-, or trimethylated in vivo, but the regulation and significance of these methylations is poorly understood. The SET domain proteins PR-Set7 and Suv4-20 have been implicated in mono- and trimethylation, respectively; however, enzymes that dimethylate lysine 20 have not been identified. Here we report that Drosophila Suv4-20 is a mixed product specificity methyltransferase that dimethylates approximately 90% and trimethylates less than 5% of total H4 at lysine 20 in S2 cells. Trimethylation, but not dimethylation, is reduced in Drosophila larvae lacking HP1, suggesting that an interaction with HP1 regulates the product specificity of Suv4-20 and enrichment of trimethyllysine 20 within heterochromatin. Similar to the Drosophila enzyme, human Suv4-20h1/h2 enzymes generate di- and trimethyllysine 20. PR-Set7 and Suv4-20 are both required for normal levels of methylation, suggesting they have non-redundant functions. Alterations in the level of lysine 20 methylation following knock-down or overexpression of Suv4-20 did not affect lysine 16 acetylation, revealing that these two modifications are not competitive in vivo. Depletion of Suv4-20h1/h2 in HeLa cells impaired the formation of 53BP1 foci, suggesting dimethyllysine 20 is required for a proper DNA damage response. Collectively, the data indicate that Suv4-20 generates nearly ubiquitous dimethylation that facilitates the DNA damage response and selective trimethylation that is involved in heterochromatin formation.

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Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle.

Project description:Methylation of histone H4 at lysine 20 (K20) has been implicated in transcriptional activation, gene silencing, heterochromatin formation, mitosis, and DNA repair. However, little is known about how this modification is regulated or how it contributes to these diverse processes. Metabolic labeling and top-down mass spectrometry reveal that newly synthesized H4 is progressively methylated at K20 during the G(2), M, and G(1) phases of the cell cycle in a process that is largely inescapable and irreversible. Approximately 98% of new H4 becomes dimethylated within two to three cell cycles, and K20 methylation turnover in vivo is undetectable. New H4 is methylated regardless of prior acetylation, and acetylation occurs predominantly on K20-dimethylated H4, refuting the hypothesis that K20 methylation antagonizes H4 acetylation and represses transcription epigenetically. Despite suggestions that it is required for normal mitosis and cell cycle progression, K20 methylation proceeds normally during colchicine treatment. Moreover, delays in PR-Set7 synthesis and K20 methylation which accompany altered cell cycle progression during sodium butyrate treatment appear to be secondary to histone hyperacetylation or other effects of butyrate since depletion of PR-Set7 did not affect cell cycle progression. Together, our data provide an unbiased perspective of the regulation and function of K20 methylation.

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