Movement dynamics of divisome proteins and PBP2x:FtsW in cells of <i>Streptococcus pneumoniae</i>.

ABSTRACT: Bacterial cell division and peptidoglycan (PG) synthesis are orchestrated by the coordinated dynamic movement of essential protein complexes. Recent studies show that bidirectional treadmilling of FtsZ filaments/bundles is tightly coupled to and limiting for both septal PG synthesis and septum closure in some bacteria, but not in others. Here we report the dynamics of FtsZ movement leading to septal and equatorial ring formation in the ovoid-shaped pathogen, Streptococcus pneumoniae Conventional and single-molecule total internal reflection fluorescence microscopy (TIRFm) showed that nascent rings of FtsZ and its anchoring and stabilizing proteins FtsA and EzrA move out from mature septal rings coincident with MapZ rings early in cell division. This mode of continuous nascent ring m

SUBMITTER: Perez AJ 

PROVIDER: S-EPMC6386697 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature