ArticleProceedings of the National Academy of Sciences of the United States of America1998
The orientation of the AP-1 heterodimer on DNA strongly affects transcriptional potency.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- New Roles of bZIP-Containing Membrane-Bound Transcription Factors in Chromatin Tethering and Karyoptosis.International journal of molecular sciences · 2025Review
- Transcription factor binding site orientation and order are major drivers of gene regulatory activity.Nature communications · 2023Article
- Strand asymmetries across genomic processes.Computational and structural biotechnology journal · 2023Review
- Detection of two isomeric binding configurations in a protein-aptamer complex with a biological nanopore.ACS nano · 2014Article
- c-Jun/c-Fos heterodimers regulate cellular genes via a newly identified class of methylated DNA sequence motifs.Nucleic acids research · 2014Article
- CpG-methylation regulates a class of Epstein-Barr virus promoters.PLoS pathogens · 2010Article
- Article
- Single nucleotide variants of the TGACTCA motif modulate energetics and orientation of binding of the Jun-Fos heterodimeric transcription factor.Biochemistry · 2009Article
- Recent computational approaches to understand gene regulation: mining gene regulation in silico.Current genomics · 2007Article
- A modified version of a Fos-associated cluster in HBZ affects Jun transcriptional potency.Nucleic acids research · 2006Article
- Distance preferences in the arrangement of binding motifs and hierarchical levels in organization of transcription regulatory information.Nucleic acids research · 2003Article
- 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
- Assembly of a functional beta interferon enhanceosome is dependent on ATF-2-c-jun heterodimer orientation.Molecular and cellular biology · 2000Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Activation of gene transcription in eukaryotes requires the cooperative assembly of an initiation complex containing many protein subunits. The necessity that these components contact each other and the promoter/enhancer in defined ways suggests that their spatial arrangement might influence the activation response. Indeed, growing evidence indicates that DNA architecture can profoundly affect transcriptional potency. Much less is known about the influence of protein architecture on transcriptional activation. Here, we examine the architectural dependence of activator function through the analysis of matched pairs of AP-1*DNA complexes differing only in their orientation. Mutation of a critical Arg residue in the basic-leucine zipper domain of either Fos or Jun yielded single point-mutant heterodimers that bind DNA in a single defined orientation, as determined directly by native chemical ligation/affinity cleavage; by contrast, the corresponding wild-type protein binds DNA as a roughly equal mixture of two isomeric orientations, which are related by subunit interchange. The stereochemistry of the point-mutant heterodimers could be switched by inversion of a C*G base pair in the center of the AP-1 site, thus providing access to both fixed orientational isomers. Yeast reporter gene assays consistently revealed that one orientational isomer activates transcription at least 10-fold more strongly than the other. These results suggest that protein architecture, especially the spatial relationship of the activation domain to the promoter, can exert a powerful influence on activator potency.
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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.