Diverse roles of TssA-like proteins in the assembly of bacterial Type VI secretion systems.

ABSTRACT: Protein translocation by the bacterial Type VI secretion system (T6SS) is driven by a rapid contraction of a sheath assembled around a tube with associated effectors. Here we show that TssA-like or TagA-like proteins with a conserved N-terminal domain and varying C-terminal domains can be grouped into at least three distinct classes based on their role in sheath assembly. The proteins of the first class increase speed and frequency of sheath assembly and form a stable dodecamer at the distal end of a polymerizing sheath. The proteins of the second class localize to the cell membrane and block sheath polymerization upon extension across the cell. This prevents excessive sheath polymerization and bending, which may result in sheath destabilization and detachment from its membrane anchor and

SUBMITTER: Johannes, P. Schneider 

PROVIDER: S-SCDT-EMBOJ-2018-100825 | biostudies-other |

REPOSITORIES: biostudies-other