ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation

• Published in: Nature (London) Vol. 405; no. 6783; pp. 195 - 200
• Main Authors: Yokoyama, Kazunari K, Kawasaki, Hiroaki, Schiltz, Lou, Chiu, Robert, Itakura, Keiichi, Taira, Kazunari, Nakatani, Yoshihiro
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 11.05.2000; Nature Publishing Group
• Subjects: Acetyltransferases - genetics; Acetyltransferases - metabolism; Activating Transcription Factor 2; Amino Acid Sequence; Animals; ATF-2 protein; Biological and medical sciences; Cyclic AMP Response Element-Binding Protein - genetics; Cyclic AMP Response Element-Binding Protein - metabolism; Enzyme Activation; Fundamental and applied biological sciences. Psychology; HeLa Cells; histone acetyltransferase; Histone Acetyltransferases; Histones - metabolism; Humans; Luciferases - genetics; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Phosphorylation; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Response Elements; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Transcription Factors - genetics; Transcription Factors - metabolism; Transcription, Genetic; Transcription. Transcription factor. Splicing. Rna processing; Acyltransferases; Histone H2B; Transcription; Enzyme; Transferases; Cyclic AMP; Response element; Histone acetyltransferase; In vitro; Histone H4; Regulation(control); Enzymatic activity; Structure activity relation; Mechanism of action
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/35012097

Transcription factors carry functional domains, which are often physically distinct, for sequence-specific DNA binding, transcriptional activation and regulatory functions. The transcription factor ATF-2 is a DNA-binding protein that binds to cyclic AMP-response elements (CREs), forms a homodimer or heterodimer with c-Jun, and stimulates CRE-dependent transcription. Here we report that ATF-2 is a histone acetyltransferase (HAT), which specifically acetylates histones H2B and H4 in vitro. Motif A, which is located in the HAT domain, is responsible for the stimulation of CRE-dependent transcription; moreover, in response to ultraviolet irradiation, phosphorylation of ATF-2 is accompanied by enhanced HAT activity of ATF-2 and CRE-dependent transcription. These results indicate that phosphorylation of ATF-2 controls its intrinsic HAT activity and its action on CRE-dependent transcription. ATF-2 may represent a new class of sequence-specific factors, which are able to activate transcription by direct effects on chromatin components.