Bacterial RNA polymerase (Acinetobacter baumannii-calcoaceticus complex) (RNAP)

Bacterial RNA polymerase (RNAP) is a multi-subunit enzyme complex essential for the transcription of DNA into RNA, a fundamental process for bacterial survival and growth (PMID: 30213815). In the Acinetobacter baumannii-calcoaceticus complex, this enzyme serves as a critical target for antimicrobial therapy, particularly given the high prevalence of multidrug resistance in these pathogens (PMID: 28804113). The core enzyme typically consists of five subunits (alpha2, beta, beta', omega) and requires a sigma factor for promoter recognition and initiation (UniProt: P0A1S2). Drugs like rifamycins bind to the beta-subunit near the active site, physically blocking the elongation of the RNA chain (PMID: 11586031). While RNAP is a validated target, its clinical utility against A. baumannii is often limited by the rapid emergence of resistance through point mutations in the rpoB gene (PMID: 25645835). Consequently, RNAP inhibitors are frequently explored as part of combination regimens to treat severe nosocomial infections such as ventilator-associated pneumonia and bloodstream infections (PMID: 29439104).

Other names

DNA-directed RNA polymeraseRNApolTranscriptaserpoB/rpoC complexRNAP

Inhibition of DNA-directed RNA polymerase activity by binding to the beta subunit (RpoB) and sterically blocking the path of the nascent RNA transcript, thereby preventing transcription elongation (PMID: 11586031).