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Section: Genetics » Expression of Gene » Transcription in Prokaryotes and Eukaryotes
 
 
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  TFIIB domains for interaction with TFIID/TATA complex
 
     
 
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Expression of Gene : Protein Synthesis 2.  Transcription in Prokaryotes and Eukaryotes
Transcription in prokaryotes 
Single RNA polymerase in E. coli
Promoter sites for initiation of transcription in prokaryotes
Initiation and elongation of RNA synthesis in prokaryotes
'Inchworm model' for elongation of transcript
Elongation arrest vs termination of transcription
Termination and antitermination of mRNA synthesis in prokaryotes
Transcription in eukaryotes 
Multiple RNA polymerases in eukaryotes
Promoter, enhancer and silencer sites for initiation of transcription in eukaryotes
Transcription factors and initiation of RNA synthesis in eukaryotes
Formation of preinitiation (transcription) complex with RNA polymerase II (Pol II)
Structure and role of TFIID and other transcription factors (TBP, TAFs)
TFIIB domains for interaction with TFIID/TATA complex
Phosphorylation of CTD of a subunit of Pol II
Formation of pre-initiation complex with Pol I and Pol III
Separate DNA binding and transcription activation domains
Transcription factors and elongation of RNA chains in eukaryotes
Chromatin structure and transcription
Transcription in mitochondria
Transcription of vertebrate mtDNA
Transcription of yeast and plant mtDNA
Transcription in chloroplasts
TFIIB domains for interaction with TFIID/TATA complex
TFIIB has two fundamental activities : (i) formation of TFIID-TFIIB/TATA complex (also called D-B DNA complex) and (ii) basal transcription. In the year 1993, deletion mutants of TFIIB were used to identify the domains responsible for the above two activities. Following two domains were identified for specific functional roles : (i) The C-terminal domain, containing two direct repeats and two basic residue repeats is necessary and sufficient for interaction with TFIID/TATA complex (also called D-DNA complex). In the absence of TFIID, TFIIB did not bind DNA suggesting that an interaction between TFIIB and TFIID takes place, (ii) An extra 84-residue N-terminal region (which is not needed for the formation of D-B complex) is required for basal transcriptional activity, so that in the absence of this region, despite the formation of D-B complex, transcription was greatly reduced or completely stopped. This region may, therefore, be involved in, the recruitment of RNA polymerase II to the complex. It has been shown that in TFIIB and TFIID, similar structural domains are present for protein-DNA interaction (these similarities include C-terminal direct repeats, basic residue repeats, sigma homologies).

It has also been shown that an acidic activator is also needed for the basal transcription activity of TFIIB. A mutant form of TFIIB, which is unable to interact with acidic activator, could not support transcription. This suggests that TFIID and TFIIB, in the absence of an acidic activator, assemble to form only a non-productive D-B complex, but form a productive D-B complex only in the presence of this acidic activator, which, transactivates the initiation complex.

 
     






     
     
 
 
     
 
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