DNA topology and a minimal set of basal factors for transcription by RNA polymerase II

Parvin, Jeffrey D.; Sharp, Phillip A.

doi:10.1016/0092-8674(93)90140-l

Cited by 383 publications

(323 citation statements)

References 38 publications

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“…As previously reported, a supercoiled template undergoes DNA unwinding more easily than a linear template, which is probably why transcription can start in the absence of TFIIH and TFIIE ( Fig. 4B; Parvin & Sharp 1993;Holstege et al 1995). TFIIE and TFIIH even stimulated transcription under these conditions (Fig.…”

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

confidence: 73%

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

confidence: 73%

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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“…This may mean that there is an excess of TFIIH in an extract or that there is more than one form of TFIIH in an extract, only one of which contains its 62-kDa subunit and binds to VP16. Alternatively, since transcriptional initiation in vitro on supercoiled DNA does not require TFIIH (76,109), transcription may not have been TFIIH dependent in some of these experiments.…”

Section: Discussionmentioning

confidence: 99%

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.

Xiao¹,

Pearson²,

Coulombe³

et al. 1994

Mol. Cell. Biol.

339

274

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Acidic transcriptional activation domains function well in both yeast and mammalian cells, and some have been shown to bind the general transcription factors TFIID and TFIIB. We now show that two acidic transactivators, herpes simplex virus VP16 and human p53, directly interact with the multisubunit human general transcription factor TFIHH and its Saccharomyces cerevisuze counterpart, factor b. The VP16-and p53-binding domains in these factors lie in the p62 subunit of TFIIH and in the homologous subunit, TFB1, of factor b. Point mutations in VP16 that reduce its transactivation activity in both yeast and mammalian cells weaken its binding to both yeast and human TFIIH. This suggests that binding of activation domains to TFIIH is an important aspect of transcriptional activation.Accurate transcription in vitro by human RNA polymerase II involves the general transcription factors TFIIA, TFIIB, TFIID, TFIIE, TFIIF (RAP30 and RAP74), TFIIH (also known as BTF2), and TFIIJ (reviewed in references 13 and 121). Beginning with TFIID, which recognizes the TATA boxes present in many promoters for RNA polymerase II, these factors and RNA polymerase II can be assembled in a defined order onto a promoter (5). TFIIH and TFIIJ are the last of these factors to bind to an assembling initiation complex (12,14,26), and TFIIH, also known as BTF2, is the only factor known to possess associated enzymatic activities. These include an ATP-dependent DNA helicase activity (95, 96) and a protein kinase activity that can phosphorylate the carboxyterminal heptapeptide repeat domain (CTD) of the largest subunit of RNA polymerase 11 (12, 21,68 herpes simplex virus transactivator VP16 (107) and in the N-terminal 73 amino acids of the mammalian tumor suppressor protein p53 (23). The p53 protein has a site-specific DNA-binding domain in its carboxy-terminal portion (101). VP16 does not, by itself, bind specifically to DNA, but instead its amino-terminal portion binds DNA in association with mammalian factors, including the POU homeodomain protein Oct-1 that recognizes octamer sequences in DNA (28,60,102). When fused to the DNA-binding domain of GAL4, the VP16 and p53 activation domains stimulate transcription in yeast and human cells of a gene bearing GAL4-binding sites (9,16,23,74,87,92). These observations imply that common mechanisms for transcriptional activation by acidic activators may exist in fungi and mammals.Many activation domains have been shown to interact with the TATA-box-binding protein (TBP) subunit of TFIID. These include the highly acidic activation domains in VP16 (50,103), p53 (10,67,72,84,97,108),118), and E2F-1 (37), as well as other kinds of activation domains found in the adenovirus activator ElA (48, 62), the Epstein-Barr virus proteins Zta (64) and R (70), the human T-cell leukemia virus type 1 (HTLV-1) activator Taxl (8), the transactivator Tat of human immunodeficiency virus type 1 (HIV-1) (53), and human c-Fos and c-Jun (85), PU-1 (38), and Spl (20). In certain cases, reduced binding of TBP by activation domains wit...

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“…Negative supercoiling is known to increase RNAPII transcription efficiency, and studies in vitro have shown that TFIIH can be dispensable for transcription initiation when there is sufficient negative supercoiling to assist in strand separation. 49,50 Therefore, the negative supercoiling from divergent transcription could prime the promoter for future initiation by facilitating DNA unwinding during the formation of an open RNAPII complex 46 (Fig. 2).…”

Section: Divergent Transcription and Negative Superhelical Tensionmentioning

confidence: 99%

Divergent transcription: A new feature of active promoters

Seila¹,

Core²,

Lis³

et al. 2009

Cell Cycle

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168

164

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DNA topology and a minimal set of basal factors for transcription by RNA polymerase II

Cited by 383 publications

References 38 publications

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

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

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.

Divergent transcription: A new feature of active promoters

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