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RNA Polymerases in Prokaryotes

RNA Polymerases in Prokaryotes - In prokaryotes a single RNA polymerase enzyme controls the synthesis of all the different types of cellular RNA. In E.coli for example, the same RNA polymerase catalyses the synthesis of mRNA, tRNA and rRNA.The entire RNA polymerase enzyme (holozyme) consists of a core enzyme and a sigma (a) factor.

In Escherchia coli and Anacytis (blue green alga) the core enzyme consists of four polypeptide chains, β, β ', α and α, and is designated as ββ’α2. In Bacillus subtilis there are seven polypeptide chains ββ’ααδω1ω2  in the core enzyme. The α chain is present twice. The sigma factor is not very firmly attached to the core enzyme and can therefore be easily isolated.

The  β’ subunit is required for the binding of RNA polymerase to the DNA template. The β’ subunit is required for binding with the sigma factor. The function of the two a subunits is not clear, but it has a possible role in promoter recognition. The function of the omega (ω) subunit, a small protein, is also not known.

It does Dot appear to be essential for normal activity of the enzyme, since the enzyme functions normally in the absence of ω. The sigma factor recognizes the start signal on the DNA template and directs the binding of RNA polymerase to the promoter region. It thus increases the specificity of core polymerase binding to DNA

The rates of synthesis of tRNA, mRNA and rRNA differ. This differential rate of synthesis is due to protein factors. One of these, the sigma factor, has already been mentioned. Another RNA polymerase factor isolated from E. coli cells infected with the bacteriophage T4 is called the T4 factor.

This stimulates the core enzyme to transcribe T4 DNA rather than bacterial DNA. yet another factor is the (psi)  factor. eThis factor isolated from E. coli causes preferential transcription of DNA coding for RNA. The psi factor does not act with the core enzyme only, but rquires the entire RNA polymerase enzyme (holoenzyme)

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