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Bacterial DNA-dependent RNA polymerase (RNAP) is a multi-subunit enzyme essential for gene expression in bacteria. It catalyzes the synthesis of all cellular RNAs by using ribonucleoside triphosphates (NTPs) as substrates and a DNA template to direct the sequence of the newly synthesized RNA. This enzyme is central to transcription, making it a critical target for regulation and antibacterial drug development. The core bacterial RNAP consists of five subunits: two alpha (α), one beta (β), one beta prime (β'), and one omega (ω) subunit. The core enzyme associates with a sigma factor (σ), forming the holoenzyme complex (α2 β β' ω σ) for promoter recognition and initiation. Bacterial RNAP transcribes all types of cellular RNA—including mRNA, tRNA, rRNA—making it indispensable for cell survival and proliferation. Bacterial RNAP is an attractive target for antibiotics like Rifamycins that bind specifically to bacterial RNAP.
Inhibition of RNA polymerase activity
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