Abstract
The RNA polymerase (RPase) holoenzyme of Escherichia coli is composed of a core enzyme with the subunit structure α2ββ′, combined with one of the multiple species of σ subunits, which provides the recognition activity for two hexanucleotide sequences of promoters, generally located near -35 and -10 positions relative to the transcription start site. The core enzyme carries all the functions necessary for RNA polymerization but the σ subunit is required for transcription initiation from promoters. Each σ subunit recognizes a different set of promoters and therefore the promoter selectivity of RPase can be modulated by replacement of the σ subunit (Helmann and Chamberlin 1988; Ishihama 1988). At present, seven different molecular species of σ subunit are known to exist in E. coli.
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Ishihama, A. (1997). Promoter Selectivity Control of RNA Polymerase. In: Eckstein, F., Lilley, D.M.J. (eds) Mechanisms of Transcription. Nucleic Acids and Molecular Biology, vol 11. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60691-5_5
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