![]() ![]() Both the function of DivIC and its recruitment to the division site depend on its extracellular domain, which interacts with the cell wall via binding to wall teichoic acids. DivIC spatially regulates peptidoglycan synthesis, and consequently cell wall architecture, by influencing the recruitment to the division septum of the major peptidoglycan synthetases PBP2 and FtsW. Here, we show a distinct, essential role for DivIC in division and survival of Staphylococcus aureus. Central to division is a transmembrane trimeric complex involving DivIB, DivIC and FtsL in Gram-positives. Many division proteins are highly conserved across bacterial species alluding to a common, basic mechanism. Bacterial cell division is a complex, dynamic process that requires multiple protein components to orchestrate its progression. ![]()
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