p300 Requires Its Histone Acetyltransferase Activity and SRC-1 Interaction Domain To Facilitate Thyroid Hormone Receptor Activation in Chromatin

doi:10.1128/MCB.20.6.2031-2042.2000

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Molecular and Cellular Biology, March 2000, p. 2031-2042, Vol. 20, No. 6
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

p300 Requires Its Histone Acetyltransferase Activity and SRC-1 Interaction Domain To Facilitate Thyroid Hormone Receptor Activation in Chromatin

Jiwen Li, Bert W. O'Malley, and Jiemin Wong^*

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030

Received 22 October 1999/Returned for modification 4 December 1999/Accepted 14 December 1999

We have characterized the mechanism by which coactivator p300 facilitates transcriptional activation mediated by the heterodimerof thyroid hormone (T3) receptor and 9-cis retinoid acid receptor(TR-RXR) in the context of chromatin. We demonstrate that, whilep300 can enhance the transcriptional activation mediated by bothliganded TR-RXR and GAL4-VP16, its histone acetyltransferase activity(HAT) is required for its ability to facilitate liganded TR-RXR-but not GAL4-VP16-mediated transcriptional activation. To understandhow p300 is recruited by liganded TR-RXR, we have analyzed theinteractions between TR-RXR and p300 as well as SRC-1 family coactivators.We show that, in contrast to a strong hormone-dependent interactionbetween TR-RXR and SRC-1 family coactivators, p300 displays minimal,if any, T3-dependent interaction with TR-RXR. However, p300 canbe recruited by liganded TR-RXR through its interaction with SRC-1family coactivators. Consistent with the protein-protein interactionprofile described above, we demonstrate that the SRC-1 interactiondomain of p300 is important for its ability to facilitate transcriptionalactivation mediated by TR-RXR, whereas its nuclear receptor interactiondomain is dispensable. Collectively, these results reveal thefunctional significance of the HAT activity of p300 and definean indirect mode for the action of p300 in TR-RXRactivation.

^* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, Baylor College of Medicine, One BaylorPlaza, Houston, TX 77030. Phone: (713) 798-6291. Fax: (713) 790-1275.E-mail: jwong{at}bcm.tmc.edu.

Molecular and Cellular Biology, March 2000, p. 2031-2042, Vol. 20, No. 6
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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