Molecular dissection of Class A PBP function uncovers novel features of the non-canonical Clostridioides difficile divisome complex.

ABSTRACT: Cell division in bacteria is mediated by the "divisome," a multiprotein complex that synthesizes the septal peptidoglycan needed to divide one cell into two. We recently showed that the major nosocomial pathogen Clostridioides difficile assembles a divisome that is fundamentally distinct from previously studied bacteria because it lacks functional orthologs of the septal peptidoglycan-synthesizing enzymes, FtsW and FtsI. While these enzymes were previously thought to mediate cell division in all walled bacteria, C. difficile instead uses the bifunctional Class A Penicillin Binding Protein PBP1 to mediate cell division. Here, we optimized a CRISPRi-based conditional expression system to define features within PBP1 that are critical for its essential functions. Our analyses identify a novel

SUBMITTER: Harrison GA 

PROVIDER: S-EPMC12539705 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature