The intrinsically disordered C-terminal linker of FtsZ regulates protofilament dynamics and superstructure in vitro.

ABSTRACT: The bacterial tubulin FtsZ polymerizes to form a discontinuous ring that drives bacterial cell division by directing local cell wall synthesis. FtsZ comprises a polymerizing GTPase domain, an intrinsically disordered C-terminal linker (CTL), and a C-terminal conserved peptide (CTC). FtsZ protofilaments align circumferentially in the cell, with the CTC mediating attachment to membrane-associated division proteins. The assembly of FtsZ protofilaments into dynamic clusters is critical for cell division, but the interactions between protofilaments and regulatory mechanisms that mediate cluster assembly and dynamics are unknown. Here, we describe a role for the CTL of Caulobacter crescentus FtsZ as an intrinsic regulator of lateral interactions between protofilaments in vitro FtsZ

SUBMITTER: Sundararajan K 

PROVIDER: S-EPMC5733589 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature