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Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity

Authors :
Tom Curran
Tsonwin Hai
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.

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