Steroid receptor coactivator-1 is a histone acetyltransferase

Thomas E. Spencer, Guido Jenster, Mark M. Burcin, C. David Allis, Jianxin Zhou, Craig A. Mizzen, Neil J. McKenna, Sergio A. Onate, Sophia Y. Tsai, Ming-Jer Tsai and Bert W. O'Malley ()
Additional contact information
Thomas E. Spencer: One Baylor Plaza, Baylor College of Medicine
Guido Jenster: One Baylor Plaza, Baylor College of Medicine
Mark M. Burcin: One Baylor Plaza, Baylor College of Medicine
C. David Allis: University of Rochester
Jianxin Zhou: University of Rochester
Craig A. Mizzen: University of Rochester
Neil J. McKenna: One Baylor Plaza, Baylor College of Medicine
Sergio A. Onate: One Baylor Plaza, Baylor College of Medicine
Sophia Y. Tsai: One Baylor Plaza, Baylor College of Medicine
Ming-Jer Tsai: One Baylor Plaza, Baylor College of Medicine
Bert W. O'Malley: One Baylor Plaza, Baylor College of Medicine

Nature, 1997, vol. 389, issue 6647, 194-198

Abstract: Abstract Steroid receptors and coactivator proteins are thought to stimulate gene expression by facilitating the assembly of basal transcription factors into a stable preinitiation complex1. What is not clear, however, is how these transcription factors gain access to transcriptionally repressed chromatin to modulate the transactivation of specific gene networks in vivo. The available evidence indicates that acetylation of chromatin in vivo is coupled to transcription and that specific histone acetyltransferases (HATs)target histones bound to DNA and overcome the inhibitory effect of chromatin on gene expression2,3,4. The steroid-receptor coactivator SRC-1 is a coactivator for many members of the steroid-hormone receptor superfamily of ligand-inducible transcription factors5. Here we show that SRC-1 possesses intrinsic histone acetyltransferase activity and that it also interacts with another HAT, p300/CBP-associated factor (PCAF). The HAT activity of SRC-1 maps to its carboxy-terminal region and is primarily specific for histones H3 and H4. Acetylation by SRC-1 and PCAF of histones bound at specific promoters may result from ligand binding to steroid receptors and could be a mechanism by which the activation functions of steroid receptors and associated coactivators enhance formation of a stable preinitiation complex, thereby increasing transcription of specific genes from transcriptionally repressed chromatin templates.

Date: 1997
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DOI: 10.1038/38304

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