Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation

O’Brien, Thomas W.; Hardin, Steven E.; Greenleaf, Arno L.; Lis, John T.

doi:10.1038/370075a0

Cited by 303 publications

(245 citation statements)

References 22 publications

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“…Although initiation of transcription is effectively complete at this stage, the CTD of RNA pol IIa must be phosphorylated in order for the transition from initiation to elongation to take place [46,47]. Phosphorylation of the CTD allows the removal of TFIIB, TFIIE and TFIIH (promoter clearance) [30,48,49], which in turn permits RNA pol IIo (phosphorylated form of RNA pol II) [49,50] to commence elongation [42].…”

Section: Figure 1 Gtf Assembly At a Typical Eukaryotic Promotermentioning

confidence: 99%

“…Phosphorylation of the CTD allows the removal of TFIIB, TFIIE and TFIIH (promoter clearance) [30,48,49], which in turn permits RNA pol IIo (phosphorylated form of RNA pol II) [49,50] to commence elongation [42]. Once elongation has been terminated, RNA pol IIo detaches from the DNA and, before it can re-enter initiation, the CTD must be dephosphorylated [47,51]. Assembly of the GTFs has been extensively reviewed in [30,49,52].…”

Section: Figure 1 Gtf Assembly At a Typical Eukaryotic Promotermentioning

confidence: 99%

“…TFIIH has a kinase activity which can phosphorylate the CTD [57], and it appears that mediator confers a 30-50-fold stimulation of this TFIIH-dependent phosphorylation [44,59]. Finally, RNA pol IIo dephosphorylation has been attributed to the holoenzyme complex [47,51,60].…”

Section: Non-structural Functions Of the Gtfsmentioning

confidence: 99%

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Transcriptional control and the role of silencers in transcriptional regulation in eukaryotes

Ogbourne

Antalis

1998

Biochemical Journal

227

171

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Mechanisms controlling transcription and its regulation are fundamental to our understanding of molecular biology and, ultimately, cellular biology. Our knowledge of transcription initiation and integral factors such as RNA polymerase is considerable, and more recently our understanding of the involvement of enhancers and complexes such as holoenzyme and mediator has increased dramatically. However, an understanding of transcriptional repression is also essential for a complete understanding of promoter structure and the regulation of gene expression. Transcriptional repression in eukaryotes is achieved through ‘silencers ’, of which there are two types, namely ‘silencer elements ’ and ‘negative regulatory elements ’ (NREs). Silencer elements are classical, position-independent elements that direct an active repression mechanism, and NREs are position-dependent elements that direct a passive repression mechanism. In addition, ‘repressors ’ are DNA-binding trasncription factors that interact directly with silencers. A review of the recent literature reveals that it is the silencer itself and its context within a given promoter, rather than the interacting repressor, that determines the mechanism of repression. Silencers form an intrinsic part of many eukaryotic promoters and, consequently, knowledge of their interactive role with enchancers and other transcriptional elements is essential for our understanding of gene regulation in eukaryotes.

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Section: Figure 1 Gtf Assembly At a Typical Eukaryotic Promotermentioning

confidence: 99%

Section: Figure 1 Gtf Assembly At a Typical Eukaryotic Promotermentioning

confidence: 99%

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Transcriptional control and the role of silencers in transcriptional regulation in eukaryotes

Ogbourne

Antalis

1998

Biochemical Journal

227

171

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“…These results indicate the special roles of the CTD in transcription and, ultimately, in ensuring cell viability. In fact, it has been reported that PolII possessing the hyperphosphorylated CTD of the largest subunit (IIo form) does not participate in the transcription PIC (Lu et al 1991), while actively transcribing PolII contains the IIo form of the largest subunit (Weeks et al 1993;O'Brien et al 1994). Recently, it was reported that the phosphorylated CTD has a role in recruiting the mRNA capping enzyme to the nascent transcript and that mRNA capping occurs soon after promoter clearance (Coppola et al 1983;Cho et al 1997;McCracken et al 1997a,b;Yue et al 1997).…”

Section: Tfiih Is the Only Kinase Active In The Transcription Preinitmentioning

confidence: 99%

Modulation of TFIIH‐associated kinase activity by complex formation and its relationship with CTD phosphorylation of RNA polymerase II

et al. 2000

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Background: The general transcription factor TFIIH plays important roles in initiation and the transition to elongation steps of transcription by RNA polymerase II (PolII). Both roles are dependent on the protein kinase, DNA-dependent ATPase and DNA helicase activities of TFIIH. However, how these enzyme activities of TFIIH contribute to transcription has remained elusive. TFIIH consists of nine subunits, and one of them, Cdk7, possesses kinase activity. Here the substrate speci®cities of TFIIH and two forms of the Cdk7-containing kinase complex are compared, and the relationship between transcription activity and the TFIIH-dependent phosphorylation of the carboxy terminal domain of the largest subunit of PolII (CTD) is studied.

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“…Through phosphorylation of the CTD, TFIIH may also be involved in the transition from an initiation complex to an elongation complex and in promoter escape (Parvin and Sharp, 1993;Goodrich and Tjian, 1994;Pan and Greenblatt, 1994;O'Brien et al, 1994). Promoter escape, which is distinct from the formation of the ®rst phosphodiester bond and typically occurs about 10 ± 40 nucleotides downstream of the initiation site (O'Brien et al, 1994), may be de®ned as the moment when elongation by RNA polymerase becomes rapid, e cient and irreversible.…”

Section: Introductionmentioning

confidence: 99%

Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH

Pearson

Greenblatt

1997

Oncogene

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The transcriptional activator E2F1 regulates the expression of genes at the G1/S boundary. We have characterized interactions of the E2F1 activation domain with two general transcription factors, the TATA-box binding protein (TBP) and TFIIH. Two distinct binding sites on E2F1 were identi®ed for TBP (amino acids 386 ± 417 and 415 ± 437) each of which supported activation in mammalian cells when expressed as a fusion to a heterologous DNA-binding domain. Neither of these minimal activation domains independently bound TFIIH; rather, the TFIIH binding site of E2F1 overlaps both domains. Loss of TFIIH-binding by E2F1 resulted in a 60 ± 65% reduction in transactivation, suggesting that the E2F1/TFIIH interaction is important, but not essential, for transactivation. The retinoblastoma protein (Rb) binds directly to E2F1 and represses E2F1-mediated transactivation. We have demonstrated that recombinant Rb can compete with TBP and the p62 subunit of TFIIH for binding to immobilized E2F1. A tumorigenic form of Rb de®cient in repressing E2F1-mediated transactivation is likewise de®cient in displacing TBP from E2F1. We propose that competition between Rb and both TBP and TFIIH for binding to E2F1 is a mechanism by which Rb inhibits transactivation by E2F1.

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Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation

Cited by 303 publications

References 22 publications

Transcriptional control and the role of silencers in transcriptional regulation in eukaryotes

Transcriptional control and the role of silencers in transcriptional regulation in eukaryotes

Modulation of TFIIH‐associated kinase activity by complex formation and its relationship with CTD phosphorylation of RNA polymerase II

Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH

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