ArticleProceedings of the National Academy of Sciences of the United States of America1998
Molecular basis of cooperative DNA bending and oriented heterodimer binding in the NFAT1-Fos-Jun-ARRE2 complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. 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, 38 citations in OpenAlex.
- Targeting the NFAT:AP-1 transcriptional complex on DNA with a small-molecule inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- 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
- Opposing roles of FoxP1 and Nfat3 in transcriptional control of cardiomyocyte hypertrophy.Molecular and cellular biology · 2011Article
- 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
- Regulation of IL-2 expression by transcription factor BACH2 in umbilical cord blood CD4+ T cells.Leukemia · 2008Article
- Protein-protein interaction analysis by C-terminally specific fluorescence labeling and fluorescence cross-correlation spectroscopy.Nucleic acids research · 2006Article
- Asymmetric recognition of nonconsensus AP-1 sites by Fos-Jun and Jun-Jun influences transcriptional cooperativity with NFAT1.Molecular and cellular biology · 2003Article
- Probing FinO-FinP RNA interactions by site-directed protein-RNA crosslinking and gelFRET.RNA (New York, N.Y.) · 2002Article
- Partners in transcription: NFAT and AP-1.Oncogene · 2001Review
- 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 glial transcription factor Sox10 binds to DNA both as monomer and dimer with different functional consequences.Nucleic acids research · 2000Article
- Assembly of a functional beta interferon enhanceosome is dependent on ATF-2-c-jun heterodimer orientation.Molecular and cellular biology · 2000Article
- Dynamic bending rigidity of a 200-bp DNA in 4 mM ionic strength: a transient polarization grating study.Biophysical journal · 2000Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cooperative DNA binding by transcription factors that bind to separate recognition sites is likely to require bending of intervening sequences and the appropriate orientation of transcription factor binding. We investigated DNA bending in complexes formed by the basic region-leucine zipper domains of Fos and Jun with the DNA binding region of nuclear factor of activated T cells 1 (NFAT1) at composite regulatory elements using gel electrophoretic phasing analysis. The NFAT1-Fos-Jun complex induced a bend at the ARRE2 site that was distinct from the sum of the bends induced by NFAT1 and Fos-Jun separately. We designate this difference DNA bending cooperativity. The bending cooperativity was directed toward the interaction interface between Fos-Jun and NFAT1. We also examined the influence of NFAT1 on the orientation of Fos-Jun heterodimer binding using a novel fluorescence resonance energy transfer assay. The interaction with NFAT1 could reverse the orientation of Fos-Jun heterodimer binding to the ARRE2 site. The principal determinants of both cooperative DNA bending and oriented heterodimer binding were localized to three amino acid residues at the amino-terminal ends of the leucine zippers of Fos and Jun. Consequently, interactions between transcription factors can remodel promoters by altering DNA bending and the orientation of heterodimer binding.
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