Bacterial DNA-directed RNA polymerase beta' subunit (β′ or beta' subunit)

The **bacterial DNA-directed RNA polymerase beta' subunit** is the largest subunit of the bacterial RNA polymerase (RNAP) core enzyme, encoded by the rpoC gene in *Escherichia coli* and many other bacteria[2][3][5]. The beta' (β′) subunit, together with the beta (β) subunit, forms the main catalytic core of the enzyme responsible for DNA-dependent RNA synthesis during transcription. The beta' subunit contains regions essential for DNA binding, catalysis, and interaction with regulatory factors and other RNAP subunits[3][4][5]. It is highly conserved among bacteria and has homologs in archaeal and eukaryotic RNA polymerases[1][6]. The beta' subunit is also a critical binding site for several classes of antibiotics, such as rifamycins, making it a validated and important antibacterial drug target[5]. Mutations in the beta' subunit can confer resistance to antibiotics that block the transcription process, underlying its role in infectious disease and antibiotic therapy. The structural and mechanistic insights into the beta' subunit have made it a focal point for antibiotic drug development as well as for understanding the fundamental mechanisms of bacterial gene expression[2][3][5].

Other names

RNAP beta' subunitRNA polymerase beta prime subunitrpoC gene product (in E. coli and other bacteria)Beta' (β′) subunit of RNA polymerase

Inhibition of RNA synthesis by binding to the beta or beta' subunit, blocking the formation of the RNA transcript or interfering with RNAP activity[2][5].