PMID- 11003650 OWN - NLM STAT- MEDLINE DCOM- 20001030 LR - 20210526 IS - 0270-7306 (Print) IS - 1098-5549 (Electronic) IS - 0270-7306 (Linking) VI - 20 IP - 20 DP - 2000 Oct TI - BRG-1 is recruited to estrogen-responsive promoters and cooperates with factors involved in histone acetylation. PG - 7541-9 AB - Several factors that mediate activation by nuclear receptors also modify the chemical and structural composition of chromatin. Prominent in this diverse group is the steroid receptor coactivator 1 (SRC-1) family, which interact with agonist-bound nuclear receptors, thereby coupling them to multifunctional transcriptional coregulators such as CREB-binding protein (CBP), p300, and PCAF, all of which have potent histone acetyltransferase activity. Additionally factors including the Brahma-related gene 1 (BRG-1) that are involved in the structural remodeling of chromatin also mediate hormone-dependent transcriptional activation by nuclear receptors. Here, we provide evidence that these two distinct mechanisms of coactivation may operate in a collaborative manner. We demonstrate that transcriptional activation by the estrogen receptor (ER) requires functional BRG-1 and that the coactivation of estrogen signaling by either SRC-1 or CBP is BRG-1 dependent. We find that in response to estrogen, ER recruits BRG-1, thereby targeting BRG-1 to the promoters of estrogen-responsive genes in a manner that occurs simultaneous to histone acetylation. Finally, we demonstrate that BRG-1-mediated coactivation of ER signaling is regulated by the state of histone acetylation within a cell. Inhibition of histone deacetylation by trichostatin A dramatically increases BRG-1-mediated coactivation of ER signaling, and this increase is reversed by overexpression of histone deacetylase 1. These studies support a critical role for BRG-1 in ER action in which estrogen stimulates an ER-BRG-1 association coupling BRG-1 to regions of chromatin at the sites of estrogen-responsive promoters and promotes the activity of other recruited factors that alter the acetylation state of chromatin. FAU - DiRenzo, J AU - DiRenzo J AD - Department of Adult Oncology, Dana Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA. FAU - Shang, Y AU - Shang Y FAU - Phelan, M AU - Phelan M FAU - Sif, S AU - Sif S FAU - Myers, M AU - Myers M FAU - Kingston, R AU - Kingston R FAU - Brown, M AU - Brown M LA - eng GR - CA57374/CA/NCI NIH HHS/United States PT - Journal Article PT - Research Support, U.S. Gov't, Non-P.H.S. PT - Research Support, U.S. Gov't, P.H.S. PL - United States TA - Mol Cell Biol JT - Molecular and cellular biology JID - 8109087 RN - 0 (Chromatin) RN - 0 (DNA-Binding Proteins) RN - 0 (Estrogens) RN - 0 (Histones) RN - 0 (Hydroxamic Acids) RN - 0 (Ligands) RN - 0 (Nuclear Proteins) RN - 0 (Receptors, Estrogen) RN - 0 (Trans-Activators) RN - 0 (Transcription Factors) RN - 3X2S926L3Z (trichostatin A) RN - EC 2.3.1.48 (CREB-Binding Protein) RN - EC 2.3.1.48 (CREBBP protein, human) RN - EC 2.3.1.48 (Histone Acetyltransferases) RN - EC 2.3.1.48 (NCOA1 protein, human) RN - EC 2.3.1.48 (Nuclear Receptor Coactivator 1) RN - EC 3.5.1.98 (Histone Deacetylases) RN - EC 3.6.1.- (SMARCA4 protein, human) RN - EC 3.6.4.- (DNA Helicases) SB - IM MH - Acetylation/drug effects MH - CREB-Binding Protein MH - Chromatin/chemistry/genetics/metabolism MH - DNA Helicases MH - DNA-Binding Proteins/metabolism MH - Estrogens/*pharmacology MH - Histone Acetyltransferases MH - Histone Deacetylases/metabolism MH - Histones/chemistry/*metabolism MH - Humans MH - Hydroxamic Acids/pharmacology MH - Ligands MH - Nuclear Proteins/*metabolism MH - Nuclear Receptor Coactivator 1 MH - Promoter Regions, Genetic/*genetics MH - Protein Binding/drug effects MH - Receptors, Estrogen/*metabolism MH - Response Elements/*genetics MH - Signal Transduction/drug effects MH - Trans-Activators/metabolism MH - Transcription Factors/*metabolism MH - Transcriptional Activation/drug effects MH - Tumor Cells, Cultured PMC - PMC86306 EDAT- 2000/09/26 11:00 MHDA- 2001/02/28 10:01 PMCR- 2000/10/01 CRDT- 2000/09/26 11:00 PHST- 2000/09/26 11:00 [pubmed] PHST- 2001/02/28 10:01 [medline] PHST- 2000/09/26 11:00 [entrez] PHST- 2000/10/01 00:00 [pmc-release] AID - 0888 [pii] AID - 10.1128/MCB.20.20.7541-7549.2000 [doi] PST - ppublish SO - Mol Cell Biol. 2000 Oct;20(20):7541-9. doi: 10.1128/MCB.20.20.7541-7549.2000.