DNA-directed RNA polymerase subunit beta-prime (bacterial RpoC) (RpoC)

DNA-directed RNA polymerase subunit beta-prime (β′) is the largest subunit of the bacterial multi-subunit RNA polymerase core enzyme, encoded by rpoC; together with the β subunit it forms the catalytic center that synthesizes RNA from a DNA template during transcription. The bacterial RNAP core comprises α2ββ′ω and associates with a sigma factor (σ) to form the holoenzyme for promoter-specific initiation. The β′ subunit contributes to the active center and mediates extensive, largely non-sequence-specific contacts with DNA and nascent RNA; in cyanobacteria and chloroplasts, β′ is split into β′ and β″ (often rpoC1 and rpoC2). As a component of the essential bacterial RNAP, β′ is part of the molecular complex targeted by antibacterial agents such as rifamycins that inhibit transcription, although rifamycins classically bind within the β subunit channel.

Other names

RNA polymerase subunit beta-primeRNAP subunit beta′Transcriptase subunit beta′rpoC gene product (Escherichia coli K-12)EC 2.7.7.6 subunit β′Beta-prime subunit of DNA-dependent RNA polymeraseIn cyanobacteria/chloroplasts: split β′ into β′ and β″ (sometimes termed rpoC1/rpoC2)

Inhibition of bacterial DNA-dependent RNA polymerase to block transcription initiation/elongation, leading to suppression of RNA synthesis and bacterial cell death or stasis (classically by rifamycins binding within the RNAP β subunit channel; activity disables the RNAP complex containing β′)