ArticleBMC molecular biology2000
High affinity binding of proteins HMG1 and HMG2 to semicatenated DNA loops.
Article in BMC molecular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- In vivo dynamics of G-quadruplex DNA structures during liver regeneration in mice.Scientific reports · 2026Article
- Progress in Assays of HMGB1 Levels in Human Plasma-The Potential Prognostic Value in COVID-19.Biomolecules · 2022Review
- Interactions of HMGB Proteins with the Genome and the Impact on Disease.Biomolecules · 2021Review
- Recognition of Local DNA Structures by p53 Protein.International journal of molecular sciences · 2017Review
- Article
- A unique HMG-box domain of mouse Maelstrom binds structured RNA but not double stranded DNA.PloS one · 2015Article
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- Article
- Inferring the choreography of parental genomes during fertilization from ultralarge-scale whole-transcriptome analysis.Genes & development · 2013Article
- Role of the acidic tail of high mobility group protein B1 (HMGB1) in protein stability and DNA bending.PloS one · 2013Article
- Methods for measuring aptamer-protein equilibria: a review.Analytica chimica acta · 2011Review
- HMGB1: the jack-of-all-trades protein is a master DNA repair mechanic.Molecular carcinogenesis · 2009Article
- A high-sensitivity method for detection and measurement of HMGB1 protein concentration by high-affinity binding to DNA hemicatenanes.PloS one · 2008Article
- Structural analysis of hemicatenated DNA loops.BMC structural biology · 2002Article
- Visualization of hemiknot DNA structure with an atomic force microscope.Nucleic acids research · 2002Article
- The DNA binding high mobility group box protein family functionally binds RNA.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundProteins HMG1 and HMG2 are two of the most abundant non histone proteins in the nucleus of mammalian cells, and contain a domain of homology with many proteins implicated in the control of development, such as the sex-determination factor Sry and the Sox family of proteins. In vitro studies of interactions of HMG1/2 with DNA have shown that these proteins can bind to many unusual DNA structures, in particular to four-way junctions, with binding affinities of 10(7) to 10(9) M(-1).
resultsHere we show that HMG1 and HMG2 bind with a much higher affinity, at least 4 orders of magnitude higher, to a new structure, Form X, which consists of a DNA loop closed at its base by a semicatenated DNA junction, forming a DNA hemicatenane. The binding constant of HMG1 to Form X is higher than 5 x 10(12) M(-1), and the half-life of the complex is longer than one hour in vitro.
conclusionsOf all DNA structures described so far with which HMG1 and HMG2 interact, we have found that Form X, a DNA loop with a semicatenated DNA junction at its base, is the structure with the highest affinity by more than 4 orders of magnitude. This suggests that, if similar structures exist in the cell nucleus, one of the functions of these proteins might be linked to the remarkable property of DNA hemicatenanes to associate two distant regions of the genome in a stable but reversible manner.
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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.