ArticleNucleic acids research2003
HMG-D and histone H1 alter the local accessibility of nucleosomal DNA.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 43 citations in OpenAlex.
- HMGB1 deforms nucleosomal DNA to generate a dynamic chromatin environment counteracting the effects of linker histone.Science advances · 2025Article
- The Role of PARP1 and PAR in ATP-Independent Nucleosome Reorganisation during the DNA Damage Response.Genes · 2022Review
- DNA breaks and chromatin structural changes enhance the transcription of autoimmune regulator target genes.The Journal of biological chemistry · 2017Article
- Single-molecule studies of high-mobility group B architectural DNA bending proteins.Biophysical reviews · 2017Review
- HMGB1 Stimulates Activity of Polymerase β on Nucleosome Substrates.Biochemistry · 2017Article
- Micronucleus-specific histone H1 is required for micronuclear chromosome integrity in Tetrahymena thermophila.PloS one · 2017Article
- Comparative analysis of linker histone H1, MeCP2, and HMGD1 on nucleosome stability and target site accessibility.Scientific reports · 2016Article
- High mobility group protein 1: A collaborator in nucleosome dynamics and estrogen-responsive gene expression.World journal of biological chemistry · 2016Review
- Genome-Wide Profiling of PARP1 Reveals an Interplay with Gene Regulatory Regions and DNA Methylation.PloS one · 2015Article
- 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
- Characterization of the interaction between HMGB1 and H3-a possible means of positioning HMGB1 in chromatin.Nucleic acids research · 2014Article
- Single-molecule kinetics reveal microscopic mechanism by which High-Mobility Group B proteins alter DNA flexibility.Nucleic acids research · 2013Article
- Quantitative proteome analysis of pluripotent cells by iTRAQ mass tagging reveals post-transcriptional regulation of proteins required for ES cell self-renewal.Molecular & cellular proteomics : MCP · 2010Article
- Biophysical characterization of DNA binding from single molecule force measurements.Physics of life reviews · 2010Review
- A translational signature for nucleosome positioning in vivo.Nucleic acids research · 2009Article
- Review
- Transient HMGB protein interactions with B-DNA duplexes and complexes.Biochemical and biophysical research communications · 2008Article
- HMGB binding to DNA: single and double box motifs.Journal of molecular biology · 2007Article
- Arabidopsis chromatin-associated HMGA and HMGB use different nuclear targeting signals and display highly dynamic localization within the nucleus.The Plant cell · 2006Article
- High-mobility-group box nuclear factors of Plasmodium falciparum.Eukaryotic cell · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There is evidence that HMGB proteins facilitate, while linker histones inhibit chromatin remodelling, respectively. We have examined the effects of HMG-D and histone H1/H5 on accessibility of nucleosomal DNA. Using the 601.2 nucleosome positioning sequence designed by Widom and colleagues we assembled nucleosomes in vitro and probed DNA accessibility with restriction enzymes in the presence or absence of HMG-D and histone H1/H5. For HMG-D our results show increased digestion at two spatially adjacent sites, the dyad and one terminus of nucleosomal DNA. Elsewhere varying degrees of protection from digestion were observed. The C-terminal acidic tail of HMG-D is essential for this pattern of accessibility. Neither the HMG domain by itself nor in combination with the adjacent basic region is sufficient. Histone H1/H5 binding produces two sites of increased digestion on opposite faces of the nucleosome and decreased digestion at all other sites. Our results provide the first evidence of local changes in the accessibility of nucleosomal DNA upon separate interaction with two linker binding proteins.
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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.