ArticleNucleic acids research2017
HMGN1 and 2 remodel core and linker histone tail domains within chromatin.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 64 citations in OpenAlex.
- High mobility group motif proteins' role in fibrosis, inflammation, and vascular injury in systemic sclerosis.Journal of molecular medicine (Berlin, Germany) · 2026Review
- Linker histone H1 represses H3 tail acetylation induced by H4 tail acetylation and alters its dynamics.Communications biology · 2026Article
- 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
- Beyond the mono-nucleosome.Biochemical Society transactions · 2025Review
- Deficiency of HMGN2 enhances antibacterial activity of macrophages by promoting H3 histone modification-mediated CD14/iNOS expression.Frontiers in immunology · 2025Article
- Identification of biomarkers and immune microenvironment associated with heart failure through bioinformatics and machine learning.Frontiers in molecular biosciences · 2025Article
- Hotspot Cancer Mutation Impairs KAT8-mediated Nucleosomal Histone Acetylation.Journal of molecular biology · 2024Article
- Article
- HMGA2 directly mediates chromatin condensation in association with neuronal fate regulation.Nature communications · 2023Article
- Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes.Journal of molecular biology · 2023Article
- Structure and Functions of HMGB2 Protein.International journal of molecular sciences · 2023Review
- HMGN1 enhances CRISPR-directed dual-function A-to-G and C-to-G base editing.Nature communications · 2023Article
- Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA.International journal of molecular sciences · 2023Article
- Next-Generation Sequencing in the Assessment of the Transcriptomic Landscape of DNA Damage Repair Genes in Abdominal Aortic Aneurysm, Chronic Venous Disease and Lower Extremity Artery Disease.International journal of molecular sciences · 2022Article
- Multiple epigenetic factors co-localize with HMGN proteins in A-compartment chromatin.Epigenetics & chromatin · 2022Article
- H3K27ac nucleosomes facilitate HMGN localization at regulatory sites to modulate chromatin binding of transcription factors.Communications biology · 2022Article
- Histone H1 Mutations in Lymphoma: A Link(er) between Chromatin Organization, Developmental Reprogramming, and Cancer.Cancer research · 2021Review
- Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021Review
- DNA sequence-dependent positioning of the linker histone in a nucleosome: A single-pair FRET study.Biophysical journal · 2021Article
- Binding of regulatory proteins to nucleosomes is modulated by dynamic histone tails.Nature communications · 2021Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The structure of the nucleosome, the basic building block of the chromatin fiber, plays a key role in epigenetic regulatory processes that affect DNA-dependent processes in the context of chromatin. Members of the HMGN family of proteins bind specifically to nucleosomes and affect chromatin structure and function, including transcription and DNA repair. To better understand the mechanisms by which HMGN 1 and 2 alter chromatin, we analyzed their effect on the organization of histone tails and linker histone H1 in nucleosomes. We find that HMGNs counteract linker histone (H1)-dependent stabilization of higher order 'tertiary' chromatin structures but do not alter the intrinsic ability of nucleosome arrays to undergo salt-induced compaction and self-association. Surprisingly, HMGNs do not displace H1s from nucleosomes; rather these proteins bind nucleosomes simultaneously with H1s without disturbing specific contacts between the H1 globular domain and nucleosomal DNA. However, HMGNs do alter the nucleosome-dependent condensation of the linker histone C-terminal domain, which is critical for stabilizing higher-order chromatin structures. Moreover, HMGNs affect the interactions of the core histone tail domains with nucleosomal DNA, redirecting the tails to more interior positions within the nucleosome. Our studies provide new insights into the molecular mechanisms whereby HMGNs affect chromatin structure.
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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.