Abstract
THE Jun proteins are nuclear proteins that combine with Fos proteins to form a gene-regulatory protein, AP-1. They have highly conserved DNA-binding and dimerization domains, resulting in almost identical sequence-recognition properties1â3. Nevertheless, there are many indications that each Jun protein activates a distinct and only partially overlapping set of AP-1 target genes4â6. Using the more variable activation domain of c-Jun as a bait, we identified a protein, JAB1, that interacts with c-Jun and JunD, but not with JunB or v-Jun. As a result, JAB1 selectively potentiates transactivation by only c-Jun or JunD. In vitro, JAB1 specifically stabilizes complexes of c-Jun or JunD with AP-1 sites and does not affect binding of either JunB or v-Jun. The amino-terminal half of JAB1 is very similar to the amino terminal region of Padl from fission yeast, which was identified genetically as a coactivator of a subset of AP-1 target genes7. JAB1 and Pad1 are also functionally interchangeable. They define a new group of coactivators that increase the specificity of target gene activation by AP-1 proteins.
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Claret, FX., Hibi, M., Dhut, S. et al. A new group of conserved coactivators that increase the specificity of AP-1 transcription factors. Nature 383, 453â457 (1996). https://doi.org/10.1038/383453a0
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DOI: https://doi.org/10.1038/383453a0
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