ArticleThe Journal of biological chemistry2012
N- and C-terminal domains determine differential nucleosomal binding geometry and affinity of linker histone isotypes H1(0) and H1c.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
- Super-resolution imaging reveals nucleolar encapsulation by single-stranded DNA.Journal of cell science · 2024Article
- Structural basis for linker histone H5-nucleosome binding and chromatin fiber compaction.Cell research · 2024Article
- Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021Review
- Molecular and Cellular Functions of the Linker Histone H1.2.Frontiers in cell and developmental biology · 2021Review
- Alternative linker histone permits fast paced nuclear divisions in early Drosophila embryo.Nucleic acids research · 2020Article
- Protein disorder-to-order transition enhances the nucleosome-binding affinity of H1.Nucleic acids research · 2020Article
- A Robust Method for the Purification and Characterization of Recombinant Human Histone H1 Variants.Biochemistry · 2019Article
- Significance of avian linker histone (H1) polymorphic variation.Journal of biosciences · 2018Review
- H1.0 Linker Histone as an Epigenetic Regulator of Cell Proliferation and Differentiation.Genes · 2018Review
- Epichromatin and chromomeres: a 'fuzzy' perspective.Open biology · 2018Review
- Linker histones: novel insights into structure-specific recognition of the nucleosome.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2017Review
- Yeast HMO1: Linker Histone Reinvented.Microbiology and molecular biology reviews : MMBR · 2017Review
- Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Chromosoma · 2017Review
- Preparative two-step purification of recombinant H1.0 linker histone and its domains.PloS one · 2017Article
- Conformational selection and dynamic adaptation upon linker histone binding to the nucleosome.Nucleic acids research · 2016Article
- Role of H1 linker histones in mammalian development and stem cell differentiation.Biochimica et biophysica acta · 2016Review
- Photobleaching studies reveal that a single amino acid polymorphism is responsible for the differential binding affinities of linker histone subtypes H1.1 and H1.5.Biology open · 2016Article
- A quantitative investigation of linker histone interactions with nucleosomes and chromatin.Scientific reports · 2016Article
- Nuclear and nucleolar activity of linker histone variant H1.0.Cellular & molecular biology letters · 2016Review
- A brief review of nucleosome structure.FEBS letters · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Eukaryotic linker or H1 histones modulate DNA compaction and gene expression in vivo. In mammals, these proteins exist as multiple isotypes with distinct properties, suggesting a functional significance to the heterogeneity. Linker histones typically have a tripartite structure composed of a conserved central globular domain flanked by a highly variable short N-terminal domain and a longer highly basic C-terminal domain. We hypothesized that the variable terminal domains of individual subtypes contribute to their functional heterogeneity by influencing chromatin binding interactions. We developed a novel dual color fluorescence recovery after photobleaching assay system in which two H1 proteins fused to spectrally separable fluorescent proteins can be co-expressed and their independent binding kinetics simultaneously monitored in a single cell. This approach was combined with domain swap and point mutagenesis to determine the roles of the terminal domains in the differential binding characteristics of the linker histone isotypes, mouse H1(0) and H1c. Exchanging the N-terminal domains between H1(0) and H1c changed their overall binding affinity to that of the other variant. In contrast, switching the C-terminal domains altered the chromatin interaction surface of the globular domain. These results indicate that linker histone subtypes bind to chromatin in an intrinsically specific manner and that the highly variable terminal domains contribute to differences between subtypes. The methods developed in this study will have broad applications in studying dynamic properties of additional histone subtypes and other mobile proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.