Faculty Opinions recommendation of Structural insights into preinitiation complex assembly on core promoters.

2021 ◽  
Author(s):  
Yunyu Shi
Keyword(s):  
Preinitiation Complex ◽  
Complex Assembly ◽  
Core Promoters ◽  
Structural Insights

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 Functional interplay between Mediator and TFIIB in preinitiation complex assembly in relation to promoter architecture

2016 ◽  
Vol 30 (18) ◽  
pp. 2119-2132 ◽  
Author(s):  
Thomas Eychenne ◽  
Elizaveta Novikova ◽  
Marie-Bénédicte Barrault ◽  
Olivier Alibert ◽  
Claire Boschiero ◽  
...  
Keyword(s):  
Preinitiation Complex ◽  
Complex Assembly ◽  
Promoter Architecture

scholarly journals Toward understanding of the mechanisms of Mediator function in vivo: Focus on the preinitiation complex assembly

Transcription ◽  
2017 ◽  
Vol 8 (5) ◽  
pp. 328-342 ◽  
Author(s):  
Thomas Eychenne ◽  
Michel Werner ◽  
Julie Soutourina
Keyword(s):  
Preinitiation Complex ◽  
Complex Assembly

scholarly journals Structural homology between the Rap30 DNA-binding domain and linker histone H5: Implications for preinitiation complex assembly

1998 ◽  
Vol 95 (16) ◽  
pp. 9117-9122 ◽  
Author(s):  
Caroline M. Groft ◽  
Sacha N. Uljon ◽  
Rong Wang ◽  
Milton H. Werner
Keyword(s):  
Dna Binding ◽  
Transcription Initiation ◽  
Linker Histone ◽  
Binding Domain ◽  
Globular Domain ◽  
Dna Binding Domain ◽  
Preinitiation Complex ◽  
Complex Assembly ◽  
Linker Histones ◽  
Histone H5

The three-dimensional structure of the human Rap30 DNA-binding domain has been solved by multinuclear NMR spectroscopy. The structure of the globular domain is strikingly similar to that of linker histone H5 and its fold places Rap30 into the “winged” helix–turn–helix family of eukaryotic transcription factors. Although the domain interacts weakly with DNA, the binding surface was identified and shown to be consistent with the structure of the HNF-3/fork head–DNA complex. The architecture of the Rap30 DNA-binding domain has important implications for the function of Rap30 in the assembly of the preinitiation complex. In analogy to the function of linker histones in chromatin formation, the fold of the Rap30 DNA-binding domain suggests that its role in transcription initiation may be that of a condensation factor for preinitiation complex assembly. Functional similarity to linker histones may explain the dependence of Rap30 binding on the bent DNA environment induced by the TATA box-binding protein. Cryptic sequence identity and functional homology between the Rap30 DNA-binding domain and region 4 of Escherichia coli σ70 may indicate that the σ factors also possess a linker histone-like activity in the formation of a prokaryotic closed complex.

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