The Interferon Antagonist ML Protein of Thogoto Virus Targets General Transcription Factor IIB

ABSTRACT The ML protein of Thogoto virus, a tick-transmitted orthomyxovirus, is a splice variant of the viral matrix protein and antagonizes the induction of antiviral type I interferon (IFN). Here we identified the general RNA polymerase II transcription factor IIB (TFIIB) as an ML-interacting protein. Overexpression of TFIIB neutralized the inhibitory effect of ML on IRF3-mediated promoter activation. Moreover, a recombinant virus expressing a mutant ML protein unable to bind TFIIB was severely impaired in its ability to suppress IFN induction. We concluded that TFIIB binding is required for the IFN antagonist effect exerted by ML. We further demonstrate that the ML-TFIIB interaction has surprisingly little impact on gene expression in general, while a strong negative effect is observed for IRF3- and NF-κB-regulated promoters.

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Interaction of the TFIIB zinc ribbon with RNA polymerase II

Biochemical Society Transactions ◽

10.1042/bst0360595 ◽

2008 ◽

Vol 36 (4) ◽

pp. 595-598 ◽

Cited By ~ 6

Author(s):

Laura M. Elsby ◽

Stefan G.E. Roberts

Keyword(s):

Transcription Factor ◽

Transcription Factors ◽

Rna Polymerase ◽

Rna Polymerase Ii ◽

Structural Models ◽

Initiation Complex ◽

General Transcription Factors ◽

Transcription Factor Iib ◽

General Transcription Factor ◽

Zinc Ribbon

Transcription by RNA polymerase II requires the assembly of the general transcription factors at the promoter to form a pre-initiation complex. The general transcription factor TF (transcription factor) IIB plays a central role in the assembly of the pre-initiation complex, providing a bridge between promoter-bound TFIID and RNA polymerase II/TFIIF. We have characterized a series of TFIIB mutants in their ability to support transcription and recruit RNA polymerase II to the promoter. Our analyses identify several residues within the TFIIB zinc ribbon that are required for RNA polymerase II assembly. Using the structural models of TFIIB, we describe the interface between the TFIIB zinc ribbon region and RNA polymerase II.

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Core promoter elements recognized by transcription factor IIB

Biochemical Society Transactions ◽

10.1042/bst0341051 ◽

2006 ◽

Vol 34 (6) ◽

pp. 1051-1053 ◽

Cited By ~ 17

Author(s):

W. Deng ◽

S.G.E. Roberts

Keyword(s):

Transcription Factor ◽

Rna Polymerase Ii ◽

Core Promoter ◽

Critical Role ◽

Tata Box ◽

Transcription Factor Iib ◽

General Transcription Factor ◽

Recognition Elements ◽

Recognition Motifs ◽

Definition Of

The general transcription factor TFIIB (transcription factor IIB) plays a critical role in the assembly of the RNA polymerase II pre-initiation complex. TFIIB can make sequence-specific DNA contacts both upstream and downstream of the TATA box. This has led to the definition of two core promoter BREs (TFIIB-recognition elements), one upstream [BREu (upstream BRE)] and one downstream of TATA box [BREd (downstream BRE)]. TFIIB–BREu and TFIIB–BREd contacts are mediated by two independent DNA-recognition motifs within the core domain of TFIIB. Both the BREu and the BREd modulate the transcriptional potency of a promoter. However, the net effect of the BREs on promoter activity is dependent on the specific blend of elements present within a core promoter.

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Position of the general transcription factor TFIIF within the RNA polymerase II transcription preinitiation complex

The EMBO Journal ◽

10.1038/emboj.2009.386 ◽

2009 ◽

Vol 29 (4) ◽

pp. 706-716 ◽

Cited By ~ 77

Author(s):

Jesse Eichner ◽

Hung-Ta Chen ◽

Linda Warfield ◽

Steven Hahn

Keyword(s):

Transcription Factor ◽

Rna Polymerase ◽

Rna Polymerase Ii ◽

Preinitiation Complex ◽

General Transcription Factor ◽

Rna Polymerase Ii Transcription

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The role of TFIIB conformation in transcriptional regulation

Biochemical Society Transactions ◽

10.1042/bst0321098 ◽

2004 ◽

Vol 32 (6) ◽

pp. 1098-1099 ◽

Cited By ~ 6

Author(s):

L.M. Elsby ◽

S.G.E. Roberts

Keyword(s):

Transcription Factor ◽

Rna Polymerase ◽

Rna Polymerase Ii ◽

Intramolecular Interaction ◽

Transcription Control ◽

Activator Proteins ◽

General Transcription Factors ◽

Transcription Factor Iib ◽

General Transcription Factor

Transcription by RNA polymerase II requires the assembly of the general transcription factors at the promoter to form a preinitiaiton complex. TFIIB (transcription factor IIB) plays a central role in this process, mediating the recruitment of RNA polymerase II and positioning it over the transcription start site. The assembly of TFIIB at the promoter can be a limiting event and several activator proteins have been shown to target TFIIB recruitment in the process of transcriptional stimulation. TFIIB is composed of two domains that engage in an intramolecular interaction. Indeed, the conformation of TFIIB has been found to underpin the function of this general transcription factor. Here we discuss our current understanding of TFIIB conformation and its role in transcription control.

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The mutationnrpb1-A325Vin the largest subunit of RNA polymerase II suppresses compromised growth ofArabidopsisplants deficient in a function of the general transcription factor IIF

The Plant Journal ◽

10.1111/tpj.13417 ◽

2017 ◽

Vol 89 (4) ◽

pp. 730-745 ◽

Cited By ~ 1

Author(s):

Elena Babiychuk ◽

Khai Trinh Hoang ◽

Klaas Vandepoele ◽

Eveline Van De Slijke ◽

Danny Geelen ◽

...

Keyword(s):

Transcription Factor ◽

Rna Polymerase ◽

Rna Polymerase Ii ◽

General Transcription Factor ◽

Transcription Factor Iif

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The general transcription factor RAP30 binds to RNA polymerase II and prevents it from binding nonspecifically to DNA

Molecular and Cellular Biology ◽

10.1128/mcb.12.1.30-37.1992 ◽

1992 ◽

Vol 12 (1) ◽

pp. 30-37

Author(s):

M T Killeen ◽

J F Greenblatt

Keyword(s):

Transcription Factor ◽

Rna Polymerase ◽

Rna Polymerase Ii ◽

Small Subunit ◽

Glutathione S Transferase ◽

General Transcription Factor ◽

Indirect Consequence ◽

Transcription In Vitro ◽

Sigma 70

RAP30/74 is a human general transcription factor that binds to RNA polymerase II and is required for initiation of transcription in vitro regardless of whether the promoter has a recognizable TATA box (Z. F. Burton, M. Killeen, M. Sopta, L. G. Ortolan, and J. F. Greenblatt, Mol. Cell. Biol. 8:1602-1613, 1988). Part of the amino acid sequence of RAP30, the small subunit of RAP30/74, has limited homology with part of Escherichia coli sigma 70 (M. Sopta, Z. F. Burton, and J. Greenblatt, Nature (London) 341:410-414, 1989). To determine which sigmalike activities of RAP30/74 could be attributed to RAP30, we purified human RAP30 and a RAP30-glutathione-S-transferase fusion protein that had been produced in E. coli. Bacterially produced RAP30 bound to RNA polymerase II in the absence of RAP74. Both partially purified natural RAP30/74 and recombinant RAP30 prevented RNA polymerase II from binding nonspecifically to DNA. In addition, nonspecific transcription by RNA polymerase II was greatly inhibited by RAP30-glutathione-S-transferase. DNA-bound RNA polymerase II could be removed from DNA by partially purified RAP30/74 but not by bacterially expressed RAP30. Thus, the ability of RAP30/74 to recruit RNA polymerase II to a promoter-bound preinitiation complex may be an indirect consequence of its ability to suppress nonspecific binding of RNA polymerase II to DNA.

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An RNA polymerase II transcription factor inactivated in poliovirus-infected cells copurifies with transcription factor TFIID

Molecular and Cellular Biology ◽

10.1128/mcb.8.8.3175-3182.1988 ◽

1988 ◽

Vol 8 (8) ◽

pp. 3175-3182

Author(s):

S Kliewer ◽

A Dasgupta

Keyword(s):

Transcription Factor ◽

Infected Cell ◽

Rna Polymerase ◽

Host Cell ◽

Rna Polymerase Ii ◽

Heat Inactivation ◽

Early Event ◽

Cell Extracts ◽

Infected Cells ◽

Rna Polymerase Ii Transcription

Inhibition of host cell RNA polymerase II-mediated transcription by poliovirus infection was studied in vitro. Whole-cell extracts prepared from poliovirus-infected HeLa cells at 3 h postinfection were shown to be deficient in a factor required for specific transcription from the adenovirus major late promoter. Three lines of evidence suggest that transcription factor TFIID is deficient in poliovirus-infected cells. First, the activity required to specifically restore transcription in poliovirus-infected cell extracts was shown to copurify with TFIID through three chromatographic steps. Second, transcription reactions reconstituted with phosphocellulose-derived chromatographic fractions revealed a fourfold decrease in the specific activity of the TFIID-containing fraction prepared from poliovirus-infected cells compared with that of the same fraction prepared from mock-infected cells. Finally, TFIID and the activity required to specifically restore transcription in virus-infected cell extracts were shown to have the same kinetics of heat inactivation. Together, these results suggest that inactivation of TFIID is an early event in the inhibition of host cell RNA polymerase II transcription by poliovirus.

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