DNA-directed RNA polymerase subunit beta (RpoB) (RpoB)

The DNA-directed RNA polymerase subunit beta (RpoB) is an essential enzyme in bacteria, serving as a core component of the RNA polymerase complex responsible for transcribing DNA into RNA [1, 11]. It plays a critical role in both the initiation and elongation phases of transcription, forming the active center for nucleotide polymerization and the exit tunnel for the nascent RNA chain [6, 8]. RpoB is the primary therapeutic target for the rifamycin class of antibiotics, including rifampicin, rifabutin, and rifapentine, which bind to a conserved pocket in the subunit to sterically block RNA elongation [1, 2, 4]. Mutations within the 81-base pair rifampicin resistance-determining region (RRDR) of the rpoB gene are the leading cause of clinical resistance in pathogens like Mycobacterium tuberculosis, necessitating the use of molecular diagnostics for patient management [3, 10, 14]. Beyond its role in infection, RpoB is a focal point for developing novel antibacterial agents to combat multidrug-resistant strains [1, 3].

Other names

RNA polymerase subunit betaRNAP subunit betaTranscriptase subunit betarpoBPlastid-encoded RNA polymerase subunit beta

Inhibition of bacterial RNA polymerase by binding to the beta subunit and sterically blocking the elongation of nascent RNA transcripts beyond a short length [1, 6, 8].