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Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
- Source :
- Proceedings of the National Academy of Sciences. 88:3720-3724
- Publication Year :
- 1991
- Publisher :
- Proceedings of the National Academy of Sciences, 1991.
-
Abstract
- The Fos/Jun and ATF/CREB families of transcription factors function in coupling extracellular signals to alterations in expression of specific target genes. Like many eukaryotic transcription factors, these proteins bind to DNA as dimers. Dimerization is mediated by a structure known as the "leucine-zipper" motif. Although Fos/Jun and ATF/CREB were previously thought to interact preferentially with different DNA regulatory elements (the AP-1/TRE and ATF/CRE sites, respectively), we find that members of these two families form selective cross-family heterodimers. The resulting heterodimers display distinguishable DNA binding specificities from each other and from their parental homodimers. These findings indicate that the Fos/Jun and ATF/CREB families of transcription factors are not as distinct as was previously thought. We suggest that they can be grouped into a superfamily of transcription factors.
- Subjects :
- Macromolecular Substances
Proto-Oncogene Proteins c-jun
Molecular Sequence Data
Oligonucleotides
Activating transcription factor
In Vitro Techniques
Regulatory Sequences, Nucleic Acid
CREB
DNA-binding protein
ATF/CREB
Structure-Activity Relationship
Proto-Oncogene Proteins
Cyclic AMP Response Element-Binding Protein
Transcription factor
Leucine Zippers
Multidisciplinary
Activating Transcription Factor 2
Base Sequence
biology
fungi
Eukaryotic transcription
Precipitin Tests
Molecular biology
Activating transcription factor 2
DNA-Binding Proteins
AP-1 transcription factor
Multigene Family
biology.protein
Proto-Oncogene Proteins c-fos
Transcription Factors
Research Article
Subjects
Details
- ISSN :
- 10916490 and 00278424
- Volume :
- 88
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences
- Accession number :
- edsair.doi.dedup.....056e48fa147f73a45ca8c91975d51368
- Full Text :
- https://doi.org/10.1073/pnas.88.9.3720