ArticleProceedings of the National Academy of Sciences of the United States of America1997
Structural basis of DNA bending and oriented heterodimer binding by the basic leucine zipper domains of Fos and Jun.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 71 citations in OpenAlex.
- Article
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- JunB condensation attenuates vascular endothelial damage under hyperglycemic condition.Journal of molecular cell biology · 2024Article
- Strand asymmetries across genomic processes.Computational and structural biotechnology journal · 2023Review
- Characterization of promoters in archaeal genomes based on DNA structural parameters.MicrobiologyOpen · 2021Article
- Promoter G-quadruplexes and transcription factors cooperate to shape the cell type-specific transcriptome.Nature communications · 2021Article
- Potential Role of Gene Regulator NFAT5 in the Pathogenesis of Diabetes Mellitus.Journal of diabetes research · 2020Review
- Flexibility and structure of flanking DNA impact transcription factor affinity for its core motif.Nucleic acids research · 2018Article
- Activator Protein-1: redox switch controlling structure and DNA-binding.Nucleic acids research · 2017Article
- Using protein-binding microarrays to study transcription factor specificity: homologs, isoforms and complexes.Briefings in functional genomics · 2015Review
- Regulation of tyrosine hydroxylase transcription by hnRNP K and DNA secondary structure.Nature communications · 2014Article
- In pursuit of design principles of regulatory sequences.Nature reviews. Genetics · 2014Review
- Genomic regions flanking E-box binding sites influence DNA binding specificity of bHLH transcription factors through DNA shape.Cell reports · 2013Article
- Opposite orientations of a transcription factor heterodimer bind DNA cooperatively with interaction partners but have different effects on interferon-β gene transcription.The Journal of biological chemistry · 2012Article
- DNA plasticity is a key determinant of the energetics of binding of Jun-Fos heterodimeric transcription factor to genetic variants of TGACGTCA motif.Biochemistry · 2009Article
- Ets-1 p51 and p42 isoforms differentially modulate Stromelysin-1 promoter according to induced DNA bend orientation.Nucleic acids research · 2009Article
- Calcineurin activates cytoglobin transcription in hypoxic myocytes.The Journal of biological chemistry · 2009Article
- Single nucleotide variants of the TGACTCA motif modulate energetics and orientation of binding of the Jun-Fos heterodimeric transcription factor.Biochemistry · 2009Article
- Mechanism of MutS searching for DNA mismatches and signaling repair.The Journal of biological chemistry · 2008Article
- Evidence that the bZIP domains of the Jun transcription factor bind to DNA as monomers prior to folding and homodimerization.Archives of biochemistry and biophysics · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interactions among transcription factors that bind to separate sequence elements require bending of the intervening DNA and juxtaposition of interacting molecular surfaces in an appropriate orientation. Here, we examine the effects of single amino acid substitutions adjacent to the basic regions of Fos and Jun as well as changes in sequences flanking the AP-1 site on DNA bending. Substitution of charged amino acid residues at positions adjacent to the basic DNA-binding domains of Fos and Jun altered DNA bending. The change in DNA bending was directly proportional to the change in net charge for all heterodimeric combinations between these proteins. Fos and Jun induced distinct DNA bends at different binding sites. Exchange of a single base pair outside of the region contacted in the x-ray crystal structure altered DNA bending. Substitution of base pairs flanking the AP-1 site had converse effects on the opposite directions of DNA bending induced by homodimers and heterodimers. These results suggest that Fos and Jun induce DNA bending in part through electrostatic interactions between amino acid residues adjacent to the basic region and base pairs flanking the AP-1 site. DNA bending by Fos and Jun at inverted binding sites indicated that heterodimers bind to the AP-1 site in a preferred orientation. Mutation of a conserved arginine within the basic regions of Fos and transversion of the central C:G base pair in the AP-1 site to G:C had complementary effects on the orientation of heterodimer binding and DNA bending. The conformational variability of the Fos-Jun-AP-1 complex may contribute to its functional versatility at different promoters.
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