The essential domain of FtsN triggers cell division by promoting interaction between FtsL and FtsI

Abstract

Cell division in bacteria requires the activation of FtsWI at the division site to synthesize septal peptidoglycan. In E. coli FtsN activates FtsWI and a previous model posited that the essential domain of FtsN (EFtsN) acts on FtsQLB causing conformational changes so that a domain of FtsL, called AWI (AWIFtsL), contacts FtsI resulting in activation of FtsW. In this study we use genetic analysis along with an AlphaFold2 model to test this activation model. Based on our findings we propose an updated model wherein theAWIFtsL and FtsI interaction is stabilized byEFtsN to activate FtsW and that this interaction is enhanced by theCytoFtsN-FtsA interaction. Thus, FtsN acts as both a sensor for divisome assembly and an activator. In addition, we elucidate the role played by two critical FtsL residues in FtsW activation.

Mycobacterium tuberculosisFtsB and PerM interact via a C-terminal helix in FtsB to modulate cell division

“…However, limitations of this MD approach, such as uncertainty in structure predictions and limited MD timescales, call for experimental validation. Importantly, in silico predictions for FtsN were corroborated by experimental results in living cells [21].…”