DNA-directed RNA polymerase (Acinetobacter baumannii) (RNAP)

DNA-directed RNA polymerase (RNAP) in Acinetobacter baumannii is a multi-subunit enzyme complex essential for the transcription of genetic information from DNA into RNA, a fundamental process for bacterial survival and growth [1, 5]. The core enzyme typically consists of five subunits (alpha2, beta, beta', and omega), which associate with a sigma factor to form the holoenzyme capable of promoter-specific initiation [27, 31]. In A. baumannii, RNAP is a critical therapeutic target, most notably for the rifamycin class of antibiotics, which bind to the beta subunit (RpoB) to sterically block the path of the elongating RNA transcript [2, 29]. Beyond its role in basic metabolism, RNAP activity is intricately linked to the pathogen's virulence and resilience, including surface-associated motility and the stringent response mediated by the alarmone (p)ppGpp [5, 44]. However, the clinical utility of targeting RNAP is often limited by the rapid emergence of resistance through point mutations in the rpoB gene, which can also lead to attenuated virulence in some strains [11, 28].

Other names

RNA polymeraseDNA-dependent RNA polymeraseTranscriptaseRNAPRpoBDNA-directed RNA polymerase holoenzyme

Inhibition of RNA synthesis by binding to the beta subunit (RpoB) of the RNA polymerase and sterically blocking the path of the elongating RNA transcript.