p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation

Kraus, W. Lee; Kadonaga, James T.

doi:10.1101/gad.12.3.331

Cited by 315 publications

(267 citation statements)

References 84 publications

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“…In vitro kinase assays Recombinant p300 and RB proteins were synthesized as described using baculoviral p300 constructs (kind gift from p300 controls G1/S transition in cancer cells NG Iyer et al Dr WL Kraus and Dr J Kadonaga) and pGEX-RB (Hagemeier et al, 1993;Kraus and Kadonaga, 1998). Recombinant RB (0.1-2 mg) was preincubated either with recombinant p300 (1-10 mg) (eluted in 10 mM TRIS pH 7.5, 0.1 % NP-40, 0.2 M NaCl, 10% glycerol, 250 mM imidazole) or equal volume carrier buffer, for 10 min at room temperature in kinase buffer (final concentration 50 mM 2-[4-(2-hydroxyethyl)-1-piperazinyl]ethanesulfonic acid pH 7.5, MgCl 2 , 1 mM dithiothreitol, 1 mM phenylmethylsulphonyl fluoride, 10 mM b-glycerophosphosphate, 10 mM adenosine 5 0 triphosphate (ATP) and 5 mM MnCl 2 ).…”

Section: Analysis Of Cell Cycle Profile and Apoptosismentioning

confidence: 99%

p300 is required for orderly G1/S transition in human cancer cells

Jian

Chin

et al. 2006

Oncogene

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Section: Analysis Of Cell Cycle Profile and Apoptosismentioning

confidence: 99%

p300 is required for orderly G1/S transition in human cancer cells

Jian

Chin

et al. 2006

Oncogene

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“…Nucleosomal arrays were generated by using recombinant Drosophila ACF complex and NAP-1 as described (15) and were confirmed by micrococcal nuclease analysis (16). (19) and His-p300(am) (20) proteins were purified by using Ni 2ϩ -NTA resin (Qiagen, Valencia, CA). The ability of the purified recombinant FL-MyoD, FL-MyoD͞MyoD, FL-MyoD͞ E47 (see Fig.…”

Section: Methodsmentioning

confidence: 99%

In vitro transcription system delineates the distinct roles of the coactivators pCAF and p300 during MyoD/E47-dependent transactivation

Dilworth

Seaver

Fishburn

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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The transcriptional coactivators p300 and pCAF are necessary for the myogenic factor MyoD to initiate the expression of skeletal muscle genes. In addition to mediating histone acetylation, both of these factors can acetylate MyoD; however, the complexity of cellular systems used to study MyoD has impeded delineation of the specific roles of these two acetyltransferases. Therefore, we established a MyoD-dependent in vitro transcription system that permits us to determine the roles of p300 and pCAF during MyoD-dependent transcriptional activation. Consistent with results from cellular systems, we demonstrate that maximal levels of transactivation in vitro require both p300 and pCAF, as well as the cofactor acetyl CoA. Dissection of the steps leading to transcription initiation revealed that the activities of p300 and pCAF are not redundant. During the initial stages of transactivation, p300 acetylates histone H3 and H4 within the promoter region and then recruits pCAF to MyoD. Once tethered to the promoter, pCAF acetylates MyoD to facilitate the transactivation process. Thus, we have established that pCAF and p300 carry out sequential and functionally distinct events on a promoter leading to transcriptional activation. Further dissection of this in vitro transcription system should be highly useful toward elucidating the mechanism by which coactivators facilitate differential gene expression by MyoD.

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“…Although recent in vitro transcription studies clearly demonstrate a functional requirement for p160͞SRC proteins, p300͞ CREB binding protein, and TRAP͞Mediator in NR-mediated gene activation (11,15,17), the question remains as to how these distinct cofactors might temporally cooperate with one another at specific target promoters. Here we examine the recruitment of TR, p160͞SRC proteins, p300, and TRAP͞Mediator at mammalian T3-responsive promoters in vivo.…”

mentioning

confidence: 99%

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

Sharma

Fondell

2002

Proc. Natl. Acad. Sci. U.S.A.

157

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Transcriptional coactivators implicated in gene activation by the thyroid hormone receptor (TR) include members of the p160͞ 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: p160͞SRC proteins and p300 are recruited first and rapidly induce histone acetylation, followed by the recruitment of the TRAP͞ Mediator complex. Interestingly, inhibition of histone deacetylase activity with trichostatin A elicited a more rapid promoter recruitment of the TRAP͞Mediator complex but not p160͞SRC 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 TRAP͞Mediator recruitment and function at specific T3-responsive mammalian promoters.T hyroid hormone receptors (TRs) are members of the nuclear receptor (NR) superfamily and regulate transcription by recruiting specific coregulatory protein complexes to target gene promoters (reviewed in refs. 1 and 2). TR binds to target promoters as a heterodimer with the retinoid X receptor (RXR) and recruits transcriptional coactivators in the presence of thyroid hormone (T3) and corepressors in the absence of T3. Coactivators that directly interact with liganded TR and facilitate transactivation include members of the p160͞steroid receptor coactivator (SRC) family (reviewed in refs. 3 and 4). These proteins are thought to function in part by associating with potent histone acetyltransferases (HATs) such as p300͞CREB binding protein and ultimately target the HAT activity to promoter-bound TR resulting in acetylation of nucleosomes. Additionally, some p160͞SRC family members contain intrinsic HAT activity (5, 6), further supporting a functional role for these factors in chromatin modification.A second type of TR coactivator is the multisubunit TRassociated protein (TRAP)͞Mediator complex (7, 8), which appears to bind liganded TR through a single subunit termed TRAP220 (9, 10). In vitro transcription assays show that TRAP͞ Mediator significantly enhances TR-dependent transcription on nonchromatin DNA templates (7,11,12), thus suggesting that the complex functions by positively influencing the basal transcription machinery, possibly by directly facilitating the recruitment of RNA polymerase II. Consistent with this view, several TRAP͞Mediator subunits share homology with proteins in yeast Mediator, a large coactivator complex that directly associates with both transcriptional activators and the yeast RNA polymerase II holoenzyme (13). Most TRAP͞Mediator subunits also have been identified in other large transcriptional coregulatory complexes, including NAT, DRIP, ARC, and CRSP (reviewed in ref. 14)...

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p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation

Cited by 315 publications

References 84 publications

p300 is required for orderly G1/S transition in human cancer cells

p300 is required for orderly G1/S transition in human cancer cells

In vitro transcription system delineates the distinct roles of the coactivators pCAF and p300 during MyoD/E47-dependent transactivation

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

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