ArticleThe EMBO journal1997
DNA bending by Fos-Jun and the orientation of heterodimer binding depend on the sequence of the AP-1 site.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 40 citations in OpenAlex.
- Article
- Mineralocorticoid Receptor (MR) trans-Activation of Inflammatory AP-1 Signaling: DEPENDENCE ON DNA SEQUENCE, MR CONFORMATION, AND AP-1 FAMILY MEMBER EXPRESSION.The Journal of biological chemistry · 2016Article
- Genomic regions flanking E-box binding sites influence DNA binding specificity of bHLH transcription factors through DNA shape.Cell reports · 2013Article
- ERK2-dependent activation of c-Jun is required for nontypeable Haemophilus influenzae-induced CXCL2 upregulation in inner ear fibrocytes.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Regulation of the human plasminogen activator inhibitor type 2 gene: cooperation of an upstream silencer and transactivator.The Journal of biological chemistry · 2012Article
- Asymmetric recognition of nonconsensus AP-1 sites by Fos-Jun and Jun-Jun influences transcriptional cooperativity with NFAT1.Molecular and cellular biology · 2003Article
- Close encounters of many kinds: Fos-Jun interactions that mediate transcription regulatory specificity.Oncogene · 2001Review
- Dynamics of Fos-Jun-NFAT1 complexes.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- The orientation of the AP-1 heterodimer on DNA strongly affects transcriptional potency.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Molecular basis of cooperative DNA bending and oriented heterodimer binding in the NFAT1-Fos-Jun-ARRE2 complex.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Effects of phosphate neutralization on the shape of the AP-1 transcription factor binding site in duplex DNA.Nucleic acids research · 1998Article
- DNA-binding domains of Fos and Jun do not induce DNA curvature: an investigation with solution and gel methods.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- DNA bending by Fos-Jun and the orientation of heterodimer binding depend on the sequence of the AP-1 site.The EMBO journal · 1997Article
- Structural basis of DNA bending and oriented heterodimer binding by the basic leucine zipper domains of Fos and Jun.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
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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
Interactions among transcription factors that bind to separate promoter elements depend on distortion of DNA structure and the appropriate orientation of transcription factor binding to allow juxtaposition of complementary structural motifs. We show that Fos and Jun induce distinct DNA bends at different binding sites, and that heterodimers bind to AP-1 sites in a preferred orientation. Sequences on each side of the consensus AP-1 recognition element have independent effects on DNA bending. A single base pair substitution outside the sequences contacted in the X-ray crystal structure alters DNA bending. Substitution of sequences flanking the AP-1 site has converse effects on DNA bending in opposite directions, suggesting that the extent of DNA bending by Fos and Jun is determined in part by the anisotropic bendability of sequences flanking the AP-1 site. DNA bending by Fos and Jun, and the orientation of heterodimer binding are interrelated. Reversal of the orientation of heterodimer binding causes a shift in the direction of DNA bending. The preferred orientation of heterodimer binding is determined both by contacts between a conserved arginine in the basic region of Fos and the central asymmetric guanine as well as the structure of sequences flanking the AP-1 site. Consequently, the structural adaptability of the Fos-Jun-AP1 complex may contribute to its functional versatility at different promoters.
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