ArticleNucleic acids research2008
Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Structural basis for linker histone H5-nucleosome binding and chromatin fiber compaction.Cell research · 2024Article
- Characterizing crosstalk in epigenetic signaling to understand disease physiology.The Biochemical journal · 2023Article
- Recent Advances in Investigating Functional Dynamics of Chromatin.Frontiers in genetics · 2022Review
- Crosstalk between H2A variant-specific modifications impacts vital cell functions.PLoS genetics · 2021Article
- Binding Dynamics of Disordered Linker Histone H1 with a Nucleosomal Particle.Journal of molecular biology · 2021Article
- Mechanism and Therapeutic Opportunities of Histone Modifications in Chronic Liver Disease.Frontiers in pharmacology · 2021Review
- Emergence of chromatin hierarchical loops from protein disorder and nucleosome asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Modelling and DNA topology of compact 2-start and 1-start chromatin fibres.Nucleic acids research · 2019Article
- Article
- A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study.Journal of biomolecular NMR · 2018Article
- Complex Evolutionary History of the Mammalian Histone H1.1-H1.5 Gene Family.Molecular biology and evolution · 2017Article
- Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Chromosoma · 2017Review
- Article
- Linker histone H1 and protein-protein interactions.Biochimica et biophysica acta · 2016Review
- Article
- The H1 linker histones: multifunctional proteins beyond the nucleosomal core particle.EMBO reports · 2015Review
- Linker histone partial phosphorylation: effects on secondary structure and chromatin condensation.Nucleic acids research · 2015Article
- Crop epigenetics and the molecular hardware of genotype × environment interactions.Frontiers in plant science · 2015Review
- Structural insights into the mechanism of negative regulation of single-box high mobility group proteins by the acidic tail domain.The Journal of biological chemistry · 2014Article
- dBigH1, a second histone H1 in Drosophila, and the consequences for histone fold nomenclature.Epigenetics · 2014Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Linker histone H1 plays an important role in chromatin folding. Phosphorylation by cyclin-dependent kinases is the main post-translational modification of histone H1. We studied the effects of phosphorylation on the secondary structure of the DNA-bound H1 carboxy-terminal domain (CTD), which contains most of the phosphorylation sites of the molecule. The effects of phosphorylation on the secondary structure of the DNA-bound CTD were site-specific and depended on the number of phosphate groups. Full phosphorylation significantly increased the proportion of beta-structure and decreased that of alpha-helix. Partial phosphorylation increased the amount of undefined structure and decreased that of alpha-helix without a significant increase in beta-structure. Phosphorylation had a moderate effect on the affinity of the CTD for the DNA, which was proportional to the number of phosphate groups. Partial phosphorylation drastically reduced the aggregation of DNA fragments by the CTD, but full phosphorylation restored to a large extent the aggregation capacity of the unphosphorylated domain. These results support the involvement of H1 hyperphosphorylation in metaphase chromatin condensation and of H1 partial phosphorylation in interphase chromatin relaxation. More generally, our results suggest that the effects of phosphorylation are mediated by specific structural changes and are not simply a consequence of the net charge.
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