Structural characterization and oligomerization of the TssL protein, a component shared by bacterial type VI and type IVb secretion systems.

ABSTRACT: The Type VI secretion system (T6SS) is a macromolecular system distributed in Gram-negative bacteria, responsible for the secretion of effector proteins into target cells. The T6SS has a broad versatility as it can target both eukaryotic and prokaryotic cells. It is therefore involved in host pathogenesis or killing neighboring bacterial cells to colonize a new niche. At the architecture level, the T6SS core apparatus is composed of 13 proteins, which assemble in two subcomplexes. One of these subcomplexes, composed of subunits that share structural similarities with bacteriophage tail and baseplate components, is anchored to the cell envelope by the membrane subcomplex. This latter is constituted of at least three proteins, TssL, TssM, and TssJ. The crystal structure of the TssJ outer mem

SUBMITTER: Durand E 

PROVIDER: S-EPMC3340138 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature