<i>Mycobacterium tuberculosis</i> FtsB and PerM interact via a C-terminal helix in FtsB to modulate cell division.

ABSTRACT: Latent infection by Mycobacterium tuberculosis (Mtb) impedes effective tuberculosis therapy and eradication. The protein PerM is essential for chronic Mtb infections in mice and acts via the divisome protein FtsB to modulate cell division. Using transgenic co-expression in Escherichia coli, we studied the Mtb PerM-FtsB interaction in isolation from other Mtb proteins, engineering PerM to enhance expression in the E. coli membrane. Using fluorescence microscopy in E. coli, we observed that the previously reported PerM-dependent instability of Mtb FtsB required a segment of FtsB predicted to bind cell-division proteins FtsL and FtsQ. Furthermore, we found that the stability of membrane-localized PerM hinged on its interaction with a conserved, C-terminal helix in

SUBMITTER: Ferreira JR 

PROVIDER: S-EPMC12004960 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature