ArticleNucleic acids research2013
Single-molecule kinetics reveal microscopic mechanism by which High-Mobility Group B proteins alter DNA flexibility.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Temporal control of Ninj1 activation determines cell-to-cell heterogeneity in IL-33 release.Communications biology · 2026Article
- HMGB1 deforms nucleosomal DNA to generate a dynamic chromatin environment counteracting the effects of linker histone.Science advances · 2025Article
- Mechanism of DNA Intercalation by Chloroquine Provides Insights into Toxicity.International journal of molecular sciences · 2024Article
- Structural domains of SARS-CoV-2 nucleocapsid protein coordinate to compact long nucleic acid substrates.Nucleic acids research · 2023Article
- New Insights into the Role of HMGB2 in ST-Segment Elevation Myocardial Infarction.International journal of general medicine · 2023Article
- Human FACT subunits coordinate to catalyze both disassembly and reassembly of nucleosomes.Cell reports · 2022Article
- HIV-1 Nucleocapsid Protein Binds Double-Stranded DNA in Multiple Modes to Regulate Compaction and Capsid Uncoating.Viruses · 2022Article
- Cisplatin fastens chromatin irreversibly even at a high chloride concentration.Nucleic acids research · 2021Article
- Virus self-assembly proceeds through contact-rich energy minima.Science advances · 2021Article
- The HMGB chromatin protein Nhp6A can bypass obstacles when traveling on DNA.Nucleic acids research · 2020Article
- Dynamics as a cause for the nanoscale organization of the genome.Nucleus (Austin, Tex.) · 2020Article
- Force-Dependent Facilitated Dissociation Can Generate Protein-DNA Catch Bonds.Biophysical journal · 2019Article
- Evidence for a bind-then-bend mechanism for architectural DNA binding protein yNhp6A.Nucleic acids research · 2019Article
- Single and double box HMGB proteins differentially destabilize nucleosomes.Nucleic acids research · 2019Article
- Acetylation and phosphorylation of human TFAM regulate TFAM-DNA interactions via contrasting mechanisms.Nucleic acids research · 2018Article
- Two-step interrogation then recognition of DNA binding site by Integration Host Factor: an architectural DNA-bending protein.Nucleic acids research · 2018Article
- Stochastic dynamics of genetic broadcasting networks.Physical review. E · 2017Article
- Article
- Single-molecule studies of high-mobility group B architectural DNA bending proteins.Biophysical reviews · 2017Review
- Molecular Mechanism of Facilitated Dissociation of Fis Protein from DNA.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Eukaryotic High-Mobility Group B (HMGB) proteins alter DNA elasticity while facilitating transcription, replication and DNA repair. We developed a new single-molecule method to probe non-specific DNA interactions for two HMGB homologs: the human HMGB2 box A domain and yeast Nhp6Ap, along with chimeric mutants replacing neutral N-terminal residues of the HMGB2 protein with cationic sequences from Nhp6Ap. Surprisingly, HMGB proteins constrain DNA winding, and this torsional constraint is released over short timescales. These measurements reveal the microscopic dissociation rates of HMGB from DNA. Separate microscopic and macroscopic (or local and non-local) unbinding rates have been previously proposed, but never independently observed. Microscopic dissociation rates for the chimeric mutants (~10 s(-1)) are higher than those observed for wild-type proteins (~0.1-1.0 s(-1)), reflecting their reduced ability to bend DNA through short-range interactions, despite their increased DNA-binding affinity. Therefore, transient local HMGB-DNA contacts dominate the DNA-bending mechanism used by these important architectural proteins to increase DNA flexibility.
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