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Publication Abstract from PubMed

Porphyromonas gingivalis, an anaerobic CFB (Cytophaga, Fusobacterium, and Bacteroides) group bacterium, is the keystone pathogen of periodontitis and has been implicated in various systemic diseases. Increased antibiotic resistance and lack of effective antibiotics necessitate a search for new intervention strategies. Here we report a 3.5 A resolution cryo-EM structure of P. gingivalis RNA polymerase (RNAP). The structure displays new structural features in its omega subunit and multiple domains in beta and beta' subunits, which differ from their counterparts in other bacterial RNAPs. Superimpositions with E. coli RNAP holoenzyme and initiation complex further suggest that its omega subunit may contact the sigma4 domain, thereby possibly contributing to the assembly and stabilization of initiation complexes. In addition to revealing the unique features of P. gingivalis RNAP, our work offers a framework for future studies of transcription regulation in this important pathogen, as well as for structure-based drug development.

Cryo-EM Structure of Porphyromonas gingivalis RNA Polymerase.,Bu F, Wang X, Li M, Ma L, Wang C, Hu Y, Cao Z, Liu B J Mol Biol. 2024 May 15;436(10):168568. doi: 10.1016/j.jmb.2024.168568. Epub 2024 , Apr 5. PMID:38583515^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.