ArticleNucleic acids research2004
The preferential binding of histone H1 to DNA scaffold-associated regions is determined by its C-terminal domain.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 43 citations in OpenAlex.
- Linker histone regulates the myeloid versus lymphoid bifurcation of multipotent hematopoietic stem and progenitors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Antimicrobial and antibiofilm activity of human recombinant H1 histones against bacterial infections.mSystems · 2024Article
- DNA sequence-dependent positioning of the linker histone in a nucleosome: A single-pair FRET study.Biophysical journal · 2021Article
- Article
- Histone H1 Post-Translational Modifications: Update and Future Perspectives.International journal of molecular sciences · 2020Review
- 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
- What is the role of histone H1 heterogeneity? A functional model emerges from a 50 year mystery.AIMS biophysics · 2015Article
- Secondary structure of protamine in sperm nuclei: an infrared spectroscopy study.BMC structural biology · 2011Article
- Nuclear tau, a key player in neuronal DNA protection.The Journal of biological chemistry · 2011Article
- Article
- Functional equivalence of HMGA- and histone H1-like domains in a bacterial transcriptional factor.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- The three methyl-CpG-binding domains of AtMBD7 control its subnuclear localization and mobility.The Journal of biological chemistry · 2008Article
- Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1.Biophysical journal · 2007Article
- Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin.BMC biology · 2007Article
- Mechanistic differences in DNA nanoparticle formation in the presence of oligolysines and poly-L-lysine.Biomacromolecules · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Histone H1 preferentially binds and aggregates scaffold-associated regions (SARs) via the numerous homopolymeric oligo(dA).oligo(dT) tracts present within these sequences. Here we show that the mammalian somatic subtypes H1a,b,c,d,e and H1 degrees and the male germline-specific subtype H1t, all preferentially bind to the Drosophila histone SAR. Experiments with the isolated domains show that whilst the C-terminal domain maintains strong and preferential binding, the N-terminal and globular domains show weak binding and poor specificity for the SAR. The preferential binding of SAR by the H1 molecule thus appears to be determined by its highly basic C-terminal domain. Salmine, a typical fish protamine, which could have its evolutionary origin in histone H1, also shows preferential binding to the SAR. The interaction of distamycin, a minor groove binder with high affinity for homopolymeric oligo(dA).oligo(dT) tracts, abolishes preferential binding of the C-terminal domain of histone H1 and protamine to the SAR, suggesting the involvement of the DNA minor groove in the interaction.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.