Phosphorylation of the Linker Histone H1 by CDK Regulates Its Binding to HP1α
Copyright policy )Phosphorylation of the Linker Histone H1 by CDK Regulates Its Binding to HP1α
Two key components of mammalian heterochromatin that play a structural role in higher order chromatin organization are the heterochromatin protein 1alpha (HP1alpha) and the linker histone H1. Here, we show that these proteins interact in vivo and in vitro through their hinge and C-terminal domains, respectively. The phosphorylation of H1 by CDK2, which is required for efficient cell cycle progression, disrupts this interaction. We propose that phosphorylation of H1 provides a signal for the disassembly of higher order chromatin structures during interphase, independent of histone H3-lysine 9 (H3-K9) methylation, by reducing the affinity of HP1alpha for heterochromatin.
- Baylor College of Medicine United States
Binding Sites, Chromosomal Proteins, Non-Histone, Recombinant Fusion Proteins, Cyclin-Dependent Kinase 2, Fluorescent Antibody Technique, Cell Biology, Chromatin, Histones, Mice, Gene Expression Regulation, Chromobox Protein Homolog 5, NIH 3T3 Cells, Tumor Cells, Cultured, Animals, Humans, Phosphorylation, Molecular Biology, Interphase, Protein Binding
Binding Sites, Chromosomal Proteins, Non-Histone, Recombinant Fusion Proteins, Cyclin-Dependent Kinase 2, Fluorescent Antibody Technique, Cell Biology, Chromatin, Histones, Mice, Gene Expression Regulation, Chromobox Protein Homolog 5, NIH 3T3 Cells, Tumor Cells, Cultured, Animals, Humans, Phosphorylation, Molecular Biology, Interphase, Protein Binding
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