Synergistic Functions of SII and p300 in Productive Activator-Dependent Transcription of Chromatin Templates

Guermah, Mohamed; Palhan, Vikas B.; Tackett, Alan J.; Chait, Brian T.; Roeder, Robert G.

doi:10.1016/j.cell.2006.01.055

Cited by 91 publications

(96 citation statements)

References 66 publications

(95 reference statements)

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“…The increased occupancy of p300 in region V is likely to be due to its association with protein complexes involved in transcription initiation, because p300 has been shown to be associated with the (Black et al, 2006) as well as with the C-terminal region of RNA polymerase II (Nakajima et al, 1997). p300 occupancy was also enriched in regions VI, VII and VIII consistent with previous reports that p300 associates with proteins involved in transcription elongation (factor SII, for example, Guermah et al, 2006;see Discussion). Interestingly, HDAC3 was also enriched wherever p300 was enriched, suggesting that p300 cooperates with HDAC3 by associating with proteins involved with transcription initiation and elongation.…”

Section: Resultssupporting

confidence: 76%

“…GST-YY1 was incubated with in vitro labeled p300C and HDAC3 together and the bound proteins were identified as above. p300 is a corepressor of c-Myc N Sankar et al TATA box and the coding regions is consistent with the recently published results showing that p300 associates with transcriptional initiation and elongation factors during gene transcription (Black et al, 2006;Guermah et al, 2006). Thus, it appears that the corepressor function of p300 is extended to the transcription initiation and coding regions where p300 appears to facilitate the recruitment of HDAC3 to the chromatin.…”

Section: Discussionsupporting

confidence: 77%

“…Thus, we overexpressed FLAG p300 in quiescent human MCF10A cells, serum stimulated for 2 h to induce Myc and then performed ChIP assays with primer pairs that encompass the upstream 647 bp of the promoter sequences ( Figure 2a shows the time course). p300 is also reported to be associated with the transcriptional initiation and elongation complexes raising the possibility that in p300 overexpressing cells, increased levels of p300 may also be found in transcriptional initiation and coding regions (Black et al, 2006;Guermah et al, 2006). Therefore, we also scanned three randomly chosen regions downstream of the RNA start site for p300 occupancy.…”

Section: Resultsmentioning

confidence: 99%

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p300 provides a corepressor function by cooperating with YY1 and HDAC3 to repress c-Myc

et al. 2008

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We showed earlier that p300/CBP plays an important role in G1 progression by negatively regulating c-Myc and thereby preventing premature G1 exit. Here, we have studied the mechanism by which p300 represses c-Myc and show that in quiescent cells p300 cooperates with histone deacetylase 3 (HDAC3) to repress transcription. p300 and HDAC3 are recruited to the upstream YY1-binding site of the c-Myc promoter resulting in chromatin deacetylation and repression of c-Myc transcription. Consistent with this, ablation of p300, YY1 or HDAC3 expression results in chromatin acetylation and induction of c-Myc. These three proteins exist as a complex in vivo and form a multiprotein complex with the YY1-binding site in vitro. The C-terminal region of p300 is both necessary and sufficient for the repression of c-Myc. These and other results suggest that in quiescent cells the C-terminal region of p300 provides corepressor function and facilitates the recruitment of p300 and HDAC3 to the YY1-binding site and represses the c-Myc promoter. This corepressor function of p300 prevents the inappropriate induction of c-Myc and S phase.

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Section: Resultssupporting

confidence: 76%

Section: Discussionsupporting

confidence: 77%

Section: Resultsmentioning

confidence: 99%

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p300 provides a corepressor function by cooperating with YY1 and HDAC3 to repress c-Myc

et al. 2008

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“…A recent study has suggested that p300 auto-acetylation serves as a switch to regulate its arrival and departure during pre-initiation complex assembly [38]. In addition, there is evidence that p300 also functions in elongation [39]. Therefore, the activity of CBP and/or p300 and their capacity to bind with certain transcriptional regulatory proteins are subjected to regulation by diverse mechanisms, hence contributing to transcriptional specificity and plasticity.…”

Section: Cbp/p300 Transcriptional Activitymentioning

confidence: 99%

Roles of CREB-binding protein (CBP)/p300 in respiratory epithelium tumorigenesis

2007

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“…They are known to stimulate transcription of specific Pol II-transcribed genes by interacting with numerous promoter-binding transcription factors that include CREB, p53, nuclear hormone receptors, and oncoprotein-related activators such as c-Fos, c-Jun, and c-Myb. The HAT function of p300/CBP was shown to be required for transcription activation in vivo (29,39) and in vitro (1,2,19,31,33). While p300/CBP has also been implicated in the stimulation of Pol I activity (20), no function in Pol III transcription has been reported to date.…”

mentioning

confidence: 99%

Different Functional Modes of p300 in Activation of RNA Polymerase III Transcription from Chromatin Templates

Mertens

Roeder

2008

Molecular and Cellular Biology

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Transcriptional coactivators that regulate the activity of human RNA polymerase III (Pol III) in the context of chromatin have not been reported. Here, we describe a completely defined in vitro system for transcription of a human tRNA gene assembled into a chromatin template. Transcriptional activation and histone acetylation in this system depend on recruitment of p300 by general initiation factor TFIIIC, thus providing a new paradigm for recruitment of histone-modifying coactivators. Beyond its role as a chromatin-modifying factor, p300 displays an acetyltransferase-independent function at the level of preinitiation complex assembly. Thus, direct interaction of p300 with TFIIIC stabilizes binding of TFIIIC to core promoter elements and results in enhanced transcriptional activity on histone-free templates. Additional studies show that p300 is recruited to the promoters of actively transcribed tRNA and U6 snRNA genes in vivo. These studies identify TFIIIC as a recruitment factor for p300 and thus may have important implications for the emerging concept that tRNA genes or TFIIIC binding sites act as chromatin barriers to prohibit spreading of silenced heterochromatin domains.It is well established that assembly of regulatory DNA sequences into nucleosomes represses transcription by restricting access of the transcriptional machinery to DNA (reviewed in reference 28). Thus, overcoming nucleosomal repression through alteration of chromatin structure is essential for gene activation. Eukaryotic cells contain at least two general classes of chromatin-modifying factors, the ATP-dependent chromatin-remodeling complexes (43) and histone-modifying enzymes that effect histone acetylation, methylation, phosphorylation, and ubiquitination (63). Whereas the function and mechanism of action of both types of factors have been extensively studied on genes transcribed by RNA polymerase II (Pol II), much less is known about chromatin-modifying factors involved in the regulation of Pol III-dependent genes.Pol III synthesizes small structural RNAs such as 5S RNA, tRNA, adenovirus VA1 RNA, and U6 RNA. Accurate and specific transcription of DNA templates by Pol III requires the assistance of the general initiation transcription factors TFIIIB and TFIIIC and, in some cases, various gene-specific factors such as the 5S gene-specific factor TFIIIA (for review, see references 15 and 53). In the case of tRNA and VA1 genes (subclass 2 genes), gene-internal core promoter elements (A and B boxes) are recognized directly by TFIIIC, which in turn directs the sequential binding of TFIIIB and Pol III. Human TFIIIC has been chromatographically separated into two distinct activities, TFIIIC1 and TFIIIC2 (74). TFIIIC2 is a stable complex of six subunits (220, 110, 102, 90,63, and 35 kDa) that binds directly to the B box (10a, 30, 75). TFIIIC1 displays no strong DNA-binding activity on its own but stabilizes TFIIIC2 binding to A and B boxes (66, 74). Other factors derived from TFIIIC preparations, such as coactivator PC4, also stabilize TFIIIC bind...

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Synergistic Functions of SII and p300 in Productive Activator-Dependent Transcription of Chromatin Templates

Cited by 91 publications

References 66 publications

p300 provides a corepressor function by cooperating with YY1 and HDAC3 to repress c-Myc

p300 provides a corepressor function by cooperating with YY1 and HDAC3 to repress c-Myc

Roles of CREB-binding protein (CBP)/p300 in respiratory epithelium tumorigenesis

Different Functional Modes of p300 in Activation of RNA Polymerase III Transcription from Chromatin Templates

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