scholarly journals Human Mediator Enhances Basal Transcription by Facilitating Recruitment of Transcription Factor IIB during Preinitiation Complex Assembly

2006 ◽  
Vol 281 (22) ◽  
pp. 15172-15181 ◽  
Author(s):  
Hwa Jin Baek ◽  
Yun Kyoung Kang ◽  
Robert G. Roeder
Keyword(s):  
Transcription Factor ◽  
Preinitiation Complex ◽  
Basal Transcription ◽  
Complex Assembly ◽  
Transcription Factor Iib

Structural insights into preinitiation complex assembly on core promoters

Science ◽  
2021 ◽  
pp. eaba8490
Author(s):  
Xizi Chen ◽  
Yilun Qi ◽  
Zihan Wu ◽  
Xinxin Wang ◽  
Jiabei Li ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Tata Box ◽  
Preinitiation Complex ◽  
Complex Assembly ◽  
Eukaryotic Transcription ◽  
Pol Ii ◽  
Core Promoters ◽  
Stepwise Assembly ◽  
Structural Insights

Transcription factor IID (TFIID) recognizes core promoters and supports preinitiation complex (PIC) assembly for RNA polymerase (Pol) II-mediated eukaryotic transcription. Here, we determined the structures of human TFIID-based PIC in three stepwise assembly states and revealed two-track PIC assembly: stepwise promoter deposition to Pol II and extensive modular reorganization on track I (on TATA-DBE promoters) versus direct promoter deposition on track II (on TATA-only and TATA-less promoters). The two tracks converge at ~50-subunit holo-PIC in identical conformation, whereby TFIID stabilizes PIC organization and supports loading (CDK)-activating kinase (CAK) onto Pol II and CAK-mediated phosphorylation of Pol II C-terminal domain. Unexpectedly, TBP of TFIID similarly bends TATA box and TATA-less promoters in PIC. Our study provides structural visualization of stepwise PIC assembly on highly diversified promoters.

scholarly journals Rapid dynamics of general transcription factor TFIIB binding during preinitiation complex assembly revealed by single-molecule analysis

2016 ◽  
Vol 30 (18) ◽  
pp. 2106-2118 ◽  
Author(s):  
Zhengjian Zhang ◽  
Brian P. English ◽  
Jonathan B. Grimm ◽  
Stephanie A. Kazane ◽  
Wenxin Hu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Single Molecule ◽  
Preinitiation Complex ◽  
Complex Assembly ◽  
General Transcription Factor ◽  
Single Molecule Analysis

Functional interaction of the v-Rel and c-Rel oncoproteins with the TATA-binding protein and association with transcription factor IIB

1993 ◽  
Vol 13 (11) ◽  
pp. 6733-6741
Author(s):  
X Xu ◽  
C Prorock ◽  
H Ishikawa ◽  
E Maldonado ◽  
Y Ito ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Basal Transcription ◽  
Transcription Factor Iib ◽  
Expression Of Genes ◽  
C Terminus ◽  
Domain Mapping

Rel family proteins regulate the expression of genes linked to kappa B-binding motifs. Little is known, however, of the mechanism by which they enhance transcription. We have investigated the ability of the v-Rel and c-Rel oncoproteins to interact with components of the basal transcription machinery. Here we report that both the acidic transcription activation domain mapping to the unique C terminus of chicken c-Rel and the F9 cell-specific activation region common to both v-Rel and c-Rel interact with the TATA-binding protein (TBP) and transcription factor IIB (TFIIB) in vitro and in vivo. We also demonstrate that TPB interaction with Rel activation regions leads to synergistic activation of transcription of a kappa B-linked reporter gene. Combined with the observation that the mouse c-Rel and human RelA proteins also interact with TBP and TFIIB in vitro, these results suggest that association with basal transcription factors is important for the transcriptional activities of Rel family proteins.

scholarly journals Structure of the τ60/Δτ91 Subcomplex of Yeast Transcription Factor IIIC: Insights into Preinitiation Complex Assembly

2006 ◽  
Vol 24 (2) ◽  
pp. 221-232 ◽  
Author(s):  
Anastasia Mylona ◽  
Carlos Fernández-Tornero ◽  
Pierre Legrand ◽  
Melina Haupt ◽  
André Sentenac ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Preinitiation Complex ◽  
Complex Assembly

scholarly journals Functional interaction of the v-Rel and c-Rel oncoproteins with the TATA-binding protein and association with transcription factor IIB.

1993 ◽  
Vol 13 (11) ◽  
pp. 6733-6741 ◽  
Author(s):  
X Xu ◽  
C Prorock ◽  
H Ishikawa ◽  
E Maldonado ◽  
Y Ito ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Basal Transcription ◽  
Transcription Factor Iib ◽  
Expression Of Genes ◽  
C Terminus ◽  
Domain Mapping

Rel family proteins regulate the expression of genes linked to kappa B-binding motifs. Little is known, however, of the mechanism by which they enhance transcription. We have investigated the ability of the v-Rel and c-Rel oncoproteins to interact with components of the basal transcription machinery. Here we report that both the acidic transcription activation domain mapping to the unique C terminus of chicken c-Rel and the F9 cell-specific activation region common to both v-Rel and c-Rel interact with the TATA-binding protein (TBP) and transcription factor IIB (TFIIB) in vitro and in vivo. We also demonstrate that TPB interaction with Rel activation regions leads to synergistic activation of transcription of a kappa B-linked reporter gene. Combined with the observation that the mouse c-Rel and human RelA proteins also interact with TBP and TFIIB in vitro, these results suggest that association with basal transcription factors is important for the transcriptional activities of Rel family proteins.

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