ArticleProceedings of the National Academy of Sciences of the United States of America1996
Fos and Jun bend the AP-1 site: effects of probe geometry on the detection of protein-induced DNA bending.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 41 citations in OpenAlex.
- DNA bending by bHLH charge variants.Nucleic acids research · 2006Article
- Inducing and modulating anisotropic DNA bends by pseudocomplementary peptide nucleic acids.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Asymmetric recognition of nonconsensus AP-1 sites by Fos-Jun and Jun-Jun influences transcriptional cooperativity with NFAT1.Molecular and cellular biology · 2003Article
- Multimerization-cyclization of DNA fragments as a method of conformational analysis.Biophysical journal · 2000Article
- Transcriptional activation by LR1 at the Emu enhancer and switch region sites.Nucleic acids research · 2000Article
- 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
- Characterization of the ATF/CREB site and its complex with GCN4.Proceedings of the National Academy of Sciences of the United States of America · 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
- Solution structure of the ATF-2 recognition site and its interaction with the ATF-2 peptide.Nucleic acids research · 1997Article
- The role of a basic amino acid cluster in target site selection and non-specific binding of bZIP peptides to DNA.Nucleic acids research · 1997Article
- 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
- DNA binding by MADS-box transcription factors: a molecular mechanism for differential DNA bending.Molecular and cellular biology · 1997Article
- Do basic region-leucine zipper proteins bend their DNA targets ... does it matter?Proceedings of the National Academy of Sciences of the United States of America · 1996Review
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1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The effect of Fos and Jun binding on the structure of the AP-1 recognition site is controversial. Results from phasing analysis and phase-sensitive detection studies of DNA bending by Fos and Jun have led to opposite conclusions. The differences between these assays, the length of the spacer between two bends and the length of the sequences flanking the bends, are investigated here using intrinsic DNA bend standards. Both an increase in the spacer length as well as a decrease in the length of flanking sequences resulted in a reduction in the phase-dependent variation in electrophoretic mobilities. Probes with a wide separation between the bends and short flanking sequences, such as those used in the phase-sensitive detection studies, displayed no phase-dependent mobility variation. This shape-dependent variation in electrophoretic mobilities was reproduced by complexes formed by truncated Fos and Jun. Results from ligase-catalyzed cyclization experiments have been interpreted to indicate the absence of DNA bending in the Fos-Jun-AP-1 complex. However, truncated Fos and Jun can alter the relative rates of inter- and intramolecular ligation through mechanisms unrelated to DNA bending, confounding the interpretation of cyclization data. The analogous phase- and shape-dependence of the electrophoretic mobilities of the Fos-Jun-AP-1 complex and an intrinsic DNA bend confirm that Fos and Jun bend DNA, which may contribute to their functions in transcription regulation.
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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.