ArticleThe EMBO journal1995
Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to four-way junction DNA.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 51 citations in OpenAlex.
- O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.Journal of the American Chemical Society · 2021Article
- The Dual Role of HMGB1 in Pancreatic Cancer.Journal of pancreatology · 2018Article
- Two high-mobility group box domains act together to underwind and kink DNA.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Histone H1 Differentially Inhibits DNA Bending by Reduced and Oxidized HMGB1 Protein.PloS one · 2015Article
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- 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
- DNA binding by single HMG box model proteins.Nucleic acids research · 2000Article
- High affinity binding of proteins HMG1 and HMG2 to semicatenated DNA loops.BMC molecular biology · 2000Article
- The high mobility group protein Abf2p influences the level of yeast mitochondrial DNA recombination intermediates in vivo.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Article
- HMG box proteins bind to four-way DNA junctions in their open conformation.The EMBO journal · 1998Article
- The HMG-box mitochondrial transcription factor xl-mtTFA binds DNA as a tetramer to activate bidirectional transcription.The EMBO journal · 1997Article
- Extracellular high-mobility group 1 protein is essential for murine erythroleukaemia cell differentiation.The Biochemical journal · 1996Article
- Identification of two DNA-binding sites on the globular domain of histone H5.The EMBO journal · 1996Article
- Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin.The EMBO journal · 1996Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Mutation of the highly conserved tryptophan residue in the A-domain HMG-box of HMG1 largely, but not completely, destroys the protein tertiary structure and abolishes its supercoiling ability, but does not abolish structure-specific DNA binding to four-way junctions. Circular dichroism shows that the protein has some residual alpha-helix (< 10%) and does not re-fold in the presence of DNA. Structure-specific DNA binding might therefore be a property of some primary structure element, for example the N-terminal extended strand, which even in the unfolded protein would be held in a restricted conformation by two, largely trans, X-Pro peptide bonds. However, mutation of P5 or P8 of the A-domain to alanine does not abolish the formation of the (first) complex in a gel retardation assay, which probably arises from binding to the junction cross-over, although the P8 mutation does affect the formation of higher complexes which may arise from binding to the junction arms. Since mutation of P8 in the W49R mutant has no effect on structure-specific junction binding, we propose that some residual alpha-helix in the protein might be involved, implicating this element in the interactions of HMG-boxes generally with DNA.
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