ArticleChromosoma2009
Site-specifically phosphorylated forms of H1.5 and H1.2 localized at distinct regions of the nucleus are related to different processes during the cell cycle.
Article in Chromosoma, 2009. 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, 50 citations in OpenAlex.
- Genetic and Epigenetic Mechanisms in Serrated Adenocarcinomas and Classical Colorectal Carcinomas: An In Silico Study.Current issues in molecular biology · 2026Article
- Integration of high-throughput proteomic data and complementary omics layers with PriOmics.Genome research · 2026Article
- Linker histone H1.5 contributes to centromere integrity.Nucleic acids research · 2026Article
- Mitapivat metabolically reprograms human β-thalassemic erythroblasts, increasing their responsiveness to oxidation.Blood advances · 2025Article
- Analysis of the interplay between MeCP2 and histone H1 duringEpigenetics · 2023Article
- Histone variant-specific post-translational modifications.Seminars in cell & developmental biology · 2023Review
- Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease.International journal of molecular sciences · 2023Review
- Structural basis of RNA polymerase II transcription on the chromatosome containing linker histone H1.Nature communications · 2022Article
- The Highest Density of Phosphorylated Histone H1 Appeared in Prophase and Prometaphase in Parallel with Reduced H3K9me3, and HDAC1 Depletion Increased H1.2/H1.3 and H1.4 Serine 38 Phosphorylation.Life (Basel, Switzerland) · 2022Article
- H1.0 C Terminal Domain Is Integral for Altering Transcription Factor Binding within Nucleosomes.Biochemistry · 2022Article
- Binding Dynamics of Disordered Linker Histone H1 with a Nucleosomal Particle.Journal of molecular biology · 2021Article
- The missing linkGenes & development · 2021Review
- Molecular and Cellular Functions of the Linker Histone H1.2.Frontiers in cell and developmental biology · 2021Review
- Site-Specific Phosphorylation of Histone H1.4 Is Associated with Transcription Activation.International journal of molecular sciences · 2020Article
- Histone H1 Post-Translational Modifications: Update and Future Perspectives.International journal of molecular sciences · 2020Review
- Phosphoprotein-based biomarkers as predictors for cancer therapy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Priming chromatin for segregation: functional roles of mitotic histone modifications.Cell cycle (Georgetown, Tex.) · 2020Review
- Emerging roles of linker histones in regulating chromatin structure and function.Nature reviews. Molecular cell biology · 2018Review
- Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Chromosoma · 2017Review
- Site-specific regulation of histone H1 phosphorylation in pluripotent cell differentiation.Epigenetics & chromatin · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell cycle-associated phosphorylation of histone H1.5 is manifested as three discrete phosphorylated forms, occurring exclusively on Ser(17), Ser(172), and Ser(188) during interphase. During late G2 and mitosis the up-phosphorylation occurs exclusively on threonine at either Thr(137) or Thr(154) to build the tetraphosphorylated forms of H1.5, whereas the pentaphosphorylated forms result from phosphorylation at Thr(10). To determine the kinetic and spatial distribution of histone H1 phosphorylation within the nucleus of synchronized Hela cells we localized three distinct phosphorylation sites of histone subtype H1.5 using affinity-purified polyclonal antibodies generated against phosphorylated Ser(17), Ser(172), and Thr(10). Immunofluorescence labeling of synchronized HeLa cells using the specific antibodies revealed that phosphorylation of H1.5 Ser(17) appeared early in G1 at discrete speckles followed by phosphorylation of Ser(172). Thr(10) phosphorylation started during prophase, showed highest phosphorylation levels during metaphase, and disappeared clearly before chromatin decondensation occurred. Experiments using the kinase inhibitor staurosporine indicate the involvement of different kinases at the various phospho-sites. Colocalization studies revealed that Ser(172) phosphorylation of H1.5 and H1.2 does colocalize to DNA replication and transcription sites. These results favor the idea that the various site-specifically phosphorylated forms of H1.5 and H1.2 localized at distinct regions of the nucleus are related to different functions during the cell cycle.
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