scholarly journals The TAFs of TFIID Bind and Rearrange the Topology of the TATA-Less RPS5 Promoter

2019 ◽  
Vol 20 (13) ◽  
pp. 3290 ◽  
Author(s):  
Sarah N. Le ◽  
Christopher R. Brown ◽  
Stacy Harvey ◽  
Hinrich Boeger ◽  
Hans Elmlund ◽  
...  
Keyword(s):  
Dna Binding ◽  
Core Promoter ◽  
Ribosomal Protein Gene ◽  
Dna Topology ◽  
Nucleosome Core ◽  
Sequence Elements ◽  
A Subunit ◽  
Promoter Dna ◽  
Tata Box Binding Protein ◽  
Tfiid Complex

The general transcription factor TFIID is a core promoter selectivity factor that recognizes DNA sequence elements and nucleates the assembly of a pre-initiation complex (PIC). The mechanism by which TFIID recognizes the promoter is poorly understood. The TATA-box binding protein (TBP) is a subunit of the multi-protein TFIID complex believed to be key in this process. We reconstituted transcription from highly purified components on a ribosomal protein gene (RPS5) and discovered that TFIIDΔTBP binds and rearranges the promoter DNA topology independent of TBP. TFIIDΔTBP binds ~200 bp of the promoter and changes the DNA topology to a larger extent than the nucleosome core particle. We show that TBP inhibits the DNA binding activities of TFIIDΔTBP and conclude that the complete TFIID complex may represent an auto-inhibited state. Furthermore, we show that the DNA binding activities of TFIIDΔTBP are required for assembly of a PIC poised to select the correct transcription start site (TSS).

TAFII250

2001 ◽  
Vol 114 (16) ◽  
pp. 2895-2902
Author(s):  
David A. Wassarman ◽  
Frank Sauer
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Activation ◽  
Messenger Rna ◽  
Structural Changes ◽  
Core Promoter ◽  
Promoter Sequence ◽  
Activator Proteins ◽  
Sequence Elements ◽  
Tata Box Binding Protein

Activation of RNA-polymerase-II-dependent transcription involves conversion of signals provided by gene-specific activator proteins into the synthesis of messenger RNA. This conversion requires dynamic structural changes in chromatin and assembly of general transcription factors (GTFs) and RNA polymerase II at core promoter sequence elements surrounding the transcription start site of genes. One hallmark of transcriptional activation is the interaction of DNA-bound activators with coactivators such as the TATA-box binding protein (TBP)-associated factors (TAFIIs) within the GTF TFIID. TAFII250 possesses a variety of activities that are likely to contribute to the initial steps of RNA polymerase II transcription. TAFII250 is a scaffold for assembly of other TAFIIs and TBP into TFIID, TAFII250 binds activators to recruit TFIID to particular promoters, TAFII250 regulates binding of TBP to DNA,TAFII250 binds core promoter initiator elements,TAFII250 binds acetylated lysine residues in core histones, and TAFII250 possesses protein kinase, ubiquitin-activating/conjugating and acetylase activities that modify histones and GTFs. We speculate that these activities achieve two goals - (1) they aid in positioning and stabilizing TFIID at particular promoters, and (2) they alter chromatin structure at the promoter to allow assembly of GTFs - and we propose a model for how TAFII250 converts activation signals into active transcription.

scholarly journals Requirement for transcription factor IIA (TFIIA)-TFIID recruitment by an activator depends on promoter structure and template competition.

1997 ◽  
Vol 17 (11) ◽  
pp. 6624-6632 ◽  
Author(s):  
P M Lieberman ◽  
J Ozer ◽  
D B Gürsel
Keyword(s):  
Transcriptional Activation ◽  
Core Promoter ◽  
Initiation Site ◽  
Transcriptional Initiation ◽  
Barr Virus ◽  
Tata Element ◽  
Epstein Barr ◽  
Substitution Mutations ◽  
Promoter Dna ◽  
Tata Box Binding Protein

Different mechanisms of transcriptional activation may be required for distinct classes of promoters and cellular conditions. The Epstein-Barr virus (EBV)-encoded transcriptional activator Zta recruits the general transcription factors IID (TFIID) and IIA (TFIIA) to promoter DNA and induces a TATA box-binding protein (TBP)-associated factor-dependent footprint downstream of the transcriptional initiation site. In this study, we investigated the functional significance of TFIID-TFIIA (D-A complex) recruitment by Zta. Alanine substitution mutations in the Zta activation domain which eliminate the ability of Zta to stimulate the D-A complex were examined. These Zta mutants were defective in the ability to activate transcription from an EBV-derived promoter (BHLF1) but activated a highly responsive synthetic promoter (Z7E4T). Both the number of activator binding sites and the core promoter region contribute to the requirement for D-A complex recruitment. These functionally distinct core promoters had significant differences in affinity for TBP and TFIID binding. The D-A complex-recruiting activity of Zta was found to be important for promoter selection in the presence of a competitor template. Conditions which limit TFIID binding to the TATA element or compromise the ability of TFIIA to bind TBP required activator stimulation of the D-A complex. These results indicate that D-A complex recruitment is one of at least two activation pathways utilized by Zta and is the essential pathway for a subset of promoters and conditions which limit TFIID binding to the TATA element.

scholarly journals Influence of promoter DNA topology on sequence-specific DNA binding and transactivation by tumor suppressor p53

Oncogene ◽  
1999 ◽  
Vol 18 (51) ◽  
pp. 7310-7318 ◽  
Author(s):  
Ella Kim ◽  
Gabor Rohaly ◽  
Stefan Heinrichs ◽  
Dimitri Gimnopoulos ◽  
Hildegard Meißner ◽  
...  
Keyword(s):  
Tumor Suppressor ◽  
Dna Binding ◽  
Dna Topology ◽  
Tumor Suppressor P53 ◽  
Promoter Dna

scholarly journals CIF150, a Human Cofactor for Transcription Factor IID-Dependent Initiator Function

1998 ◽  
Vol 18 (1) ◽  
pp. 233-239 ◽  
Author(s):  
Jörg Kaufmann ◽  
Katharina Ahrens ◽  
Ronald Koop ◽  
Stephen T. Smale ◽  
Rolf Müller
Keyword(s):  
Transcription Factor ◽  
Core Promoter ◽  
Direct Interaction ◽  
Striking Similarity ◽  
Binding Assays ◽  
Vitro Binding ◽  
Transcription Factor Iid ◽  
Tata Box Binding Protein ◽  
Tfiid Complex

ABSTRACT The transcription factor IID (TFIID) complex is highly conserved between the Drosophila and mammalian systems. A mammalian homolog has been described for all the Drosophila TATA box-binding protein-associated factors (TAFs), with the exception of dTAFII150. We previously reported the identification of CIF, an essential cofactor for TFIID-dependent transcription from promoters containing initiator (Inr) elements. Here we describe the molecular cloning of CIF150, the human homolog of dTAFII150, and present biochemical evidence that this factor is involved in Inr activity. CIF150 is capable of mediating TFIID-dependent Inr activity in a complementation assay, and a protein fraction lacking Inr activity lacks detectable amounts of CIF150. Despite the striking similarity to dTAFII150, CIF150 does not appear to be associated with human TFIID. However, in vitro binding assays revealed a specific and direct interaction between CIF150 and hTAFII135. This interaction might be structurally important for the functional interaction between CIF150 and human TFIID, since CIF150 stabilizes TFIID binding to a core promoter.

scholarly journals Structure of human TFIID and mechanism of TBP loading onto promoter DNA

Science ◽  
2018 ◽  
Vol 362 (6421) ◽  
pp. eaau8872 ◽  
Author(s):  
Avinash B. Patel ◽  
Robert K. Louder ◽  
Basil J. Greber ◽  
Sebastian Grünberg ◽  
Jie Luo ◽  
...  
Keyword(s):  
Core Promoter ◽  
Mechanistic Model ◽  
Tata Box ◽  
Molecular Architecture ◽  
Eukaryotic Transcription ◽  
General Transcription Factor ◽  
Specific Loading ◽  
Promoter Dna ◽  
Tata Box Binding Protein ◽  
Initial Binding

The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo–electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box–binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter.

scholarly journals Two related ARID family proteins are alternative subunits of human SWI/SNF complexes

2004 ◽  
Vol 383 (2) ◽  
pp. 319-325 ◽  
Author(s):  
Xiaomei WANG ◽  
Norman G. NAGL ◽  
Deborah WILSKER ◽  
Michael VAN SCOY ◽  
Stephen PACCHIONE ◽  
...  
Keyword(s):  
Dna Binding ◽  
Direct Evidence ◽  
Potential Interaction ◽  
Atpase Subunit ◽  
Reading Frame ◽  
Atpase Subunits ◽  
A Subunit ◽  
Distinct Subunit ◽  
Binding Behaviour

p270 (ARID1A) is a member of the ARID family of DNA-binding proteins and a subunit of human SWI/SNF-related complexes, which use the energy generated by an integral ATPase subunit to remodel chromatin. ARID1B is an independent gene product with an open reading frame that is more than 60% identical with p270. We have generated monoclonal antibodies specific for either p270 or ARID1B to facilitate the investigation of ARID1B and its potential interaction with human SWI/SNF complexes in vivo. Immunocomplex analysis provides direct evidence that endogenous ARID1B is associated with SWI/SNF-related complexes and indicates that p270 and ARID1B, similar to the ATPase subunits BRG1 and hBRM, are alternative, mutually exclusive subunits of the complexes. The ARID-containing subunits are not specific to the ATPases. Each associates with both BRG1 and hBRM, thus increasing the number of distinct subunit combinations known to be present in cells. Analysis of the panels of cell lines indicates that ARID1B, similar to p270, has a broad tissue distribution. The ratio of p270/ARID1B in typical cells is approx. 3.5:1, and BRG1 is distributed proportionally between the two ARID subunits. Analysis of DNA-binding behaviour indicates that ARID1B binds DNA in a non-sequence-specific manner similar to p270.

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