Impacts of local and global sequence patterns within the disordered tail on assembly and functions of B. subtilis FtsZ

Abstract

FtsZ is one of the main drivers of bacterial cell division. In the presence of GTP, FtsZ assembles into treadmilling polymers that serve as a platform for assembly of the division machinery. In B. subtilis, the C-terminal tail of FtsZ is encompasses a 50 aa linker (CTL) that is hypervariable across orthologs and a conserved C-terminal peptide (CTP). Deletion of the intrinsically disordered C-terminal tail of FtsZ compromises cell division and leads to a deleterious phenotype in B. subtilis. Biochemical experiments showed that the CTL and the CTP enable autoregulation of FtsZ polymerization and GTPase activity.