scholarly journals Beyond the canonical role of TFIIB in eukaryotic transcription

2021 ◽  
Author(s):  
Michael J. O’Brien ◽  
Athar Ansari
Keyword(s):  
Eukaryotic Transcription

scholarly journals Leading role of TBP in the Establishment of Complexity in Eukaryotic Transcription Initiation Systems

Cell Reports ◽  
2017 ◽  
Vol 21 (13) ◽  
pp. 3941-3956 ◽  
Author(s):  
Eiryo Kawakami ◽  
Naruhiko Adachi ◽  
Toshiya Senda ◽  
Masami Horikoshi
Keyword(s):  
Transcription Initiation ◽  
Eukaryotic Transcription ◽  
Leading Role

The mechanistic role of enhancer elements in eukaryotic transcription

BioEssays ◽  
1988 ◽  
Vol 8 (4) ◽  
pp. 104-107 ◽  
Author(s):  
Kuan-Teh Jeang ◽  
George Khoury
Keyword(s):  
Eukaryotic Transcription

scholarly journals Cdk9 regulates a promoter-proximal checkpoint to modulate RNA Polymerase II elongation rate

2017 ◽  
Author(s):  
Gregory T. Booth ◽  
Pabitra K. Parua ◽  
Miriam Sansó ◽  
Robert P. Fisher ◽  
John T. Lis
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Time Course ◽  
Kinase Activity ◽  
Elongation Rate ◽  
Transcription Start ◽  
Eukaryotic Transcription ◽  
Pol Ii ◽  
Cdk9 Kinase Activity

Multiple kinases modify RNA Polymerase II (Pol II) and its associated pausing and elongation factors to regulate Pol II transcription and transcription-coupled mRNA processing1,2. The conserved Cdk9 kinase is essential for regulated eukaryotic transcription3, but its mechanistic role remains incompletely understood. Here, we use altered-specificity kinase mutations and highly-specific inhibitors in fission yeast, Schizosaccharomyces pombe to examine the role of Cdk9, and related Cdk7 and Cdk12 kinases, on transcription at base-pair resolution using Precision Run-On sequencing (PRO-seq). Within a minute, Cdk9 inhibition causes a dramatic reduction in the phosphorylation of Pol II-associated factor, Spt5. The effects of Cdk9 inhibition on transcription are the more severe than inhibition of Cdk7 and Cdk12 and result in a shift of Pol II towards the transcription start site (TSS). A kinetic time course of Cdk9 inhibition reveals that early transcribing Pol II is the most compromised, with a measured rate of only ~400 bp/min, while Pol II that is already well into the gene continues rapidly to the end of genes with a rate > 1 kb/min. Our results indicate that while Pol II in S. pombe can escape promoter-proximal pausing in the absence of Cdk9 activity, it is impaired in elongation, suggesting the existence of a conserved global regulatory checkpoint that requires Cdk9 kinase activity.

scholarly journals Transcription Factor E Is a Part of Transcription Elongation Complexes

2007 ◽  
Vol 282 (49) ◽  
pp. 35482-35490 ◽  
Author(s):  
Sebastian Grünberg ◽  
Michael S. Bartlett ◽  
Souad Naji ◽  
Michael Thomm
Keyword(s):  
Transcription Factor ◽  
Terminal Part ◽  
Eukaryotic Transcription ◽  
Α Subunit ◽  
Winged Helix ◽  
Transcription Bubble ◽  
Template Strand ◽  
Transcription Complexes ◽  
Dna Strand

A homologue of the N-terminal domain of the α subunit of the general eukaryotic transcription factor TFE is encoded in the genomes of all sequenced archaea, but the position of archaeal TFE in transcription complexes has not yet been defined. We show here that TFE binds nonspecifically to single-stranded DNA, and photochemical cross-linking revealed TFE binding to a preformed open transcription bubble. In preinitiation complexes, the N-terminal part of TFE containing a winged helix-turn-helix motif is cross-linked specifically to DNA of the nontemplate DNA strand at positions –9 and –11. In complexes stalled at +20, TFE cross-linked specifically to positions +9, +11, and +16 of the non-template strand. Analyses of transcription complexes stalled at position +20 revealed a TFE-dependent increase of the resumption efficiency of stalled RNA polymerase and a TFE-induced enhanced permanganate sensitivity of thymine residues in the transcription bubble. These results demonstrate the presence of TFE in early elongation complexes and suggest a role of TFE in stabilization of the transcription bubble during elongation.

Role of multiprotein bridging factor 1 in archaea: bridging the domains?

2009 ◽  
Vol 37 (1) ◽  
pp. 52-57 ◽  
Author(s):  
Bart de Koning ◽  
Fabian Blombach ◽  
Hao Wu ◽  
Stan J.J. Brouns ◽  
John van der Oost
Keyword(s):  
Yeast Genome ◽  
Terminal Part ◽  
Context Analysis ◽  
Eukaryotic Transcription ◽  
Translation Fidelity ◽  
Genome Context Analysis ◽  
Tata Box Binding Protein ◽  
Genome Context ◽  
Regulatory Dna

MBF1 (multiprotein bridging factor 1) is a highly conserved protein in archaea and eukaryotes. It was originally identified as a mediator of the eukaryotic transcription regulator BmFTZ-F1 (Bombyx mori regulator of fushi tarazu). MBF1 was demonstrated to enhance transcription by forming a bridge between distinct regulatory DNA-binding proteins and the TATA-box-binding protein. MBF1 consists of two parts: a C-terminal part that contains a highly conserved helix–turn–helix, and an N-terminal part that shows a clear divergence: in eukaryotes, it is a weakly conserved flexible domain, whereas, in archaea, it is a conserved zinc-ribbon domain. Although its function in archaea remains elusive, its function as a transcriptional co-activator has been deduced from thorough studies of several eukaryotic proteins, often indicating a role in stress response. In addition, MBF1 was found to influence translation fidelity in yeast. Genome context analysis of mbf1 in archaea revealed conserved clustering in the crenarchaeal branch together with genes generally involved in gene expression. It points to a role of MBF1 in transcription and/or translation. Experimental data are required to allow comparison of the archaeal MBF1 with its eukaryotic counterpart.

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