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ATF-2 is a DNA-binding protein that binds to cAMP-response elements (CREs) and forms a hetrodimer with c-Jun, via binding of the leucine zipper motif and then stimulates the CRE-dependent transcription (1,2). Recently, we have reported that ATF-2 has an intrinsic acetyltransferase activity that is controlled by phosphorylation. Mutant form of either p300 or ATF-2 with mutations in the HAT domain failed to stimulate the CRE-dependent transcription in response to UV irradiation. Moreover, phosphorylation of ATF-2 enhanced its HAT activity and CRE-dependent transcription. Thus, these results indicate that HAT activity of ATF-2 is important for the CRE-dependent transcription.

Histone acetyltransferase (HAT) activity of ATF-2 is necessary for the CRE-dependent transcription