ArticleNucleic acids research2000
DNA binding by single HMG box model proteins.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Enhanced genome-wide association reveals the role of YABBY11-NGATHA-LIKE1 in leaf serration development of Populus.Plant physiology · 2023Article
- The extracellular innate-immune effector HMGB1 limits pathogenic bacterial biofilm proliferation.The Journal of clinical investigation · 2021Article
- Conformation and protein interactions of intramolecular DNA and phosphorothioate four-way junctions.Experimental biology and medicine (Maywood, N.J.) · 2021Article
- Characterization of the structural and protein recognition properties of hybrid PNA-DNA four-way junctions.Archives of biochemistry and biophysics · 2015Article
- A unique HMG-box domain of mouse Maelstrom binds structured RNA but not double stranded DNA.PloS one · 2015Article
- Interaction of HMG proteins and H1 with hybrid PNA-DNA junctions.Protein science : a publication of the Protein Society · 2013Article
- Cooperative recruitment of HMGB1 during V(D)J recombination through interactions with RAG1 and DNA.Nucleic acids research · 2013Article
- Interactions of recombinant HMGB proteins with branched RNA substrates.Biochemical and biophysical research communications · 2008Article
- Mating type protein Mat1-2 from asexual Aspergillus fumigatus drives sexual reproduction in fertile Aspergillus nidulans.Eukaryotic cell · 2008Article
- Isolation and characterization of a cDNA encoding a putative high mobility group (HMG)--box protein from stored mRNA in resting cysts of the ciliate Oxytricha (Sterkiella) nova: ciliate macronuclear gene encoding a putative HMG-box protein.Molecular biology reports · 2003Article
- Mutagenesis of the HMGB (high-mobility group B) protein Cmb1 (cytosine-mismatch binding 1) of Schizosaccharomyces pombe: effects on recognition of DNA mismatches and damage.The Biochemical journal · 2003Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The HMG1/2 family is a large group of proteins that share a conserved sequence of approximately 80 amino acids rich in basic, aromatic and proline side chains, referred to as an HMG box. Previous studies show that HMG boxes can bind to DNA in a structure-specific manner. To define the basis for DNA recognition by HMG boxes, we characterize the interaction of two model HMG boxes, one a structure-specific box, rHMGb from the rat HMG1 protein, the other a sequence-specific box, Rox1 from yeast, with oligodeoxynucleotide substrates. Both proteins interact with single-stranded oligonucleotides in this study to form 1:1 complexes. The stoichiometry of binding of rHMGb to duplex or branched DNAs differs: for a 16mer duplex we find a weak 2:1 complex, while a 4:1 protein:DNA complex is detected with a four-way DNA junction of 16mers in the presence of Mg(2+). In the case of the sequence-specific Rox1 protein we find tight 1:1 and 2:1 complexes with its cognate duplex sequence and again a 4:1 complex with four-way branched DNA. If the DNA branching is reduced to three arms, both proteins form 3:1 complexes. We believe that these multimeric complexes are relevant for HMG1/2 proteins in vivo, since Mg(2+) is present in the nucleus and these proteins are expressed at a very high level.
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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.