General Transcription Factor IIB Overexpression and a Potential Link to Proliferation in Human Hepatocellular Carcinoma

2012 ◽  
Vol 19 (2) ◽  
pp. 195-203 ◽  
Author(s):  
Liren Li ◽  
Aixian Zhang ◽  
Xiaolei Cao ◽  
Jing Chen ◽  
Yunfei Xia ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Transcription Factor ◽  
Human Hepatocellular Carcinoma ◽  
Transcription Factor Iib ◽  
General Transcription Factor ◽  
Potential Link

scholarly journals Targeting the mevalonate pathway is a novel therapeutic approach to inhibit oncogenic FoxM1 transcription factor in human hepatocellular carcinoma

Oncotarget ◽  
2018 ◽  
Vol 9 (30) ◽  
pp. 21022-21035 ◽  
Author(s):  
Satoshi Ogura ◽  
Yuichi Yoshida ◽  
Tomohide Kurahashi ◽  
Mayumi Egawa ◽  
Kunimaro Furuta ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Transcription Factor ◽  
Therapeutic Approach ◽  
Mevalonate Pathway ◽  
Human Hepatocellular Carcinoma ◽  
Novel Therapeutic

Interaction of the TFIIB zinc ribbon with RNA polymerase II

2008 ◽  
Vol 36 (4) ◽  
pp. 595-598 ◽  
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.

Core promoter elements recognized by transcription factor IIB

2006 ◽  
Vol 34 (6) ◽  
pp. 1051-1053 ◽  
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.

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

2008 ◽  
Vol 82 (22) ◽  
pp. 11446-11453 ◽  
Author(s):  
Carola Vogt ◽  
Ellen Preuss ◽  
Daniel Mayer ◽  
Friedemann Weber ◽  
Martin Schwemmle ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase Ii ◽  
Matrix Protein ◽  
Inhibitory Effect ◽  
Type I ◽  
Interacting Protein ◽  
Transcription Factor Iib ◽  
General Transcription Factor ◽  
Negative Effect ◽  
Rna Polymerase Ii Transcription

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.

Sign in / Sign up

Export Citation Format

Share Document