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Section: Genetics » Expression of Gene » Transcription in Prokaryotes and Eukaryotes
 
 
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  Multiple RNA polymerases in eukaryotes
 
     
 
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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


Transcription in Eukaryotes
Multiple RNA polymerases in eukaryotes
In eukaryotes there are atleast three different nuclear RNA polymerases, whose properties are given in Table 32.2.

The three RNA polymerases can be distinguished on the basis of their sensitivity to certain inhibitors of transcription, e.g. α amanitin. Each of these enzymes is a large protein (~500,000 daltons), with two large and several (8 < 10) smaller subunits, some of them showing homology to the subunits of E. coll RNA polymerase. The largest subunit (~200,000 daltons) has homology with β', and the second large subunit (- 140,000 daltons) has homology with β subunit of E. coli RNA polymerase (Fig. 32.2). One small subunit of RNA polymerase II also has homology with α subunit. The second largest subunit of RNA polymerase II also shares the catalytic sites of ribonucleases, which may be used for RNA cleavage and may thus help in proof reading (Fig. 32.12).
 
A model of the structure of prokaryotic RNA polymerase showing association of five polypeptides (α2ββ').
Fig. 32.2. A model of the structure of prokaryotic RNA polymerase showing association of five polypeptides (α2ββ').

Functional regions of the second largest subunit of RNA polymerase II of Drosophila. Solid bar shows similarity with barnase and other bacterial RNAses; A to I are regions having homology with prokaryotic RNA polymerase.
Fig. 32.12. Functional regions of the second largest subunit of RNA polymerase II of Drosophila. Solid bar shows similarity with barnase and other bacterial RNAses; A to I are regions having homology with prokaryotic RNA polymerase.

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