ArticleBiochemistry2011
HU binding to a DNA four-way junction probed by Förster resonance energy transfer.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Long-lived pauses reveal tunable kinetic barriers during Holliday junction migration.Nucleic acids research · 2026Article
- Article
- Site-Specific Investigation of DNA Holliday Junction Dynamics and Structure with 6-Methylisoxanthopterin, a Fluorescent Guanine Analog.bioRxiv : the preprint server for biology · 2024Article
- Non-specific and specific DNA binding modes of bacterial histone, HU, separately regulate distinct physiological processes through different mechanisms.Molecular microbiology · 2023Article
- Site-specific investigation of DNA Holliday Junction dynamics and structure with 6-Methylisoxanthopterin, a fluorescent guanine analog.Trends in photochemistry & photobiology · 2023Article
- Integration Host Factor Binds DNA Holliday Junctions.International journal of molecular sciences · 2022Article
- Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features.Journal of visualized experiments : JoVE · 2022Article
- The extracellular innate-immune effector HMGB1 limits pathogenic bacterial biofilm proliferation.The Journal of clinical investigation · 2021Article
- The extracellular DNA lattice of bacterial biofilms is structurally related to Holliday junction recombination intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- MutSγ-Induced DNA Conformational Changes Provide Insights into Its Role in Meiotic Recombination.Biophysical journal · 2018Article
- Fluorescently labeled circular DNA molecules for DNA topology and topoisomerases.Scientific reports · 2016Article
- HU multimerization shift controls nucleoid compaction.Science advances · 2016Article
- Holliday Junction Thermodynamics and Structure: Coarse-Grained Simulations and Experiments.Scientific reports · 2016Article
- Probing the Ion Binding Site in a DNA Holliday Junction Using Förster Resonance Energy Transfer (FRET).International journal of molecular sciences · 2016Article
- Article
- Cooperative recruitment of HMGB1 during V(D)J recombination through interactions with RAG1 and DNA.Nucleic acids research · 2013Article
- Noncoding RNAs binding to the nucleoid protein HU in Escherichia coli.Journal of bacteriology · 2012Article
- Holliday junction affinity of the base excision repair factor Endo III contributes to cholera toxin phage integration.The EMBO journal · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The Escherichia coli protein HU is a non-sequence-specific DNA-binding protein that interacts with DNA primarily through electrostatic interactions. In addition to nonspecific binding to linear DNA, HU has been shown to bind with nanomolar affinity to discontinuous DNA substrates, such as repair and recombination intermediates. This work specifically examines the HU-four-way junction (4WJ) interaction using fluorescence spectroscopic methods. The conformation of the junction in the presence of different counterions was investigated by Förster resonance energy transfer (FRET) measurements, which revealed an ion-type conformational dependence, where Na(+) yields the most stacked conformation followed by K(+) and Mg(2+). HU binding induces a greater degree of stacking in the Na(+)-stabilized and Mg(2+)-stabilized junctions but not the K(+)-stabilized junction, which is attributed to differences in the size of the ionic radii and potential differences in ion binding sites. Interestingly, junction conformation modulates binding affinity, where HU exhibits the lowest affinity for the Mg(2+)-stabilized form (24 μM(-1)), which is the least stacked conformation. Protein binding to a mixed population of open and stacked forms of the junction leads to nearly complete formation of a protein-stabilized stacked-X junction. These results strongly support a model in which HU binds to and stabilizes the stacked-X conformation.
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