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All of the classes of RNA in bacteria are transcribed by a single RNA polymerase. This RNA polymerase is a multisubunit protein that has two forms: holoenzyme (with sigma factor) and core polymerase (without sigma factor). The antibiotic Rifampicin (derived from rifamycin), which is used to treat tuberculosis among other things, inhibits the beta subunit of RNA polymerase. Sigma factor functions as an initiation factor. Since there are a number of different species of sigma factor in E. coli, they can provide some selectivity for certain classes of genes. Sigma factor functions to facilitate the binding of RNA polymerase to promoters. As shown in the table, the core polymerase has high affinity for any DNA. This, however, would slow down the search for a promoter by slowing down the trial and error search for promoter DNA. The holoenzyme, in contrast, has reduced affinity for any DNA and greatly increased affinity for promoter DNA. Thus, sigma factor allows a very rapid search for promoters, and ensures that RNA polymerase will stably bind, once a promoter is found. The role that is played by sigma factor in the sigma cycle is shown here. Sigma factor first helps RNA polymerase to find the promoter by binding to the -10 region. This is only moderately stable as a closed (duplex DNA) complex, but becomes highly stable as an open (melted DNA) complex. Sigma factor binding helps to denature the A-T rich TATAAT Pribnow box forming the open complex. Once initiation takes place, sigma factor dissociates, freeing the core RNA polymerase from the very high affinity interaction at the promoter, thus allowing it to move away from the promoter to transcribe the rest of the gene. Sigma factor is then free to re-bind other core RNA polymerase enzymes. * Common Points Same basic principles (base pairs et al); Promoter site as the initiation site; Similar elongation; Takes one strand of DNA as template strand; Does not require a primer; Occurs in the 5’-3’ dir
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