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Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo

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Sharma, Dipali, Fondell, Joseph D.·2002·Proceedings of the National Academy of Sciences

Abstract

Transcriptional coactivators implicated in gene activation by the thyroid hormone receptor (TR) include members of the p160/steroid receptor coactivator (SRC) family of proteins, p300, and the multisubunit TR-associated protein (TRAP)/Mediator complex. We investigated the temporal recruitment of these cofactors to mammalian thyroid hormone (T3)-responsive promoters in vivo . We show that upon T3 treatment, TR recruits all three types of coactivators to specific promoters in at least two sequential steps: p160/SRC proteins and p300 are recruited first and rapidly induce histone acetylation, followed by the recruitment of the TRAP/Mediator complex. Interestingly, inhibition of histone deacetylase activity with trichostatin A elicited a more rapid promoter recruitment of the TRAP/Mediator complex but not p160/SRC proteins. T3-dependent gene expression assays indicate that all three coactivators are targeted to a promoter before significant activation occurs. These findings thus suggest that histone acetylation may be a prerequisite for TRAP/Mediator recruitment and function at specific T3-responsive mammalian promoters.

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Metadata

Authors
Sharma, D., & Fondell, J. D.
Venue
Proceedings of the National Academy of Sciences
Published
2002-05-28
Volume
99
Issue
12
Pages
7934-7939
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1967632442
Cited by
160
References
4
FWCI
5.18
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo. https://app.cochat.ai/papers/10.1073/pnas.122004799
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Sharma, D., & Fondell, J. D. (2002). Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.122004799

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