ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation
ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation
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DOI:
10.1038/35012097
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发表时间:
2000-05-11
期刊:
影响因子:
64.8
通讯作者:
Yokoyama, KK
中科院分区:
文献类型:
--
作者:
Kawasaki, H;Schiltz, L;Yokoyama, KK
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(1-3). 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.