The C‐tail anchored TssL subunit, an essential protein of the enteroaggregative Escherichia coli Sci‐1 Type VI secretion system, is inserted by YidC

• DOI: 10.1002/mbo3.9
• Publication Date: 2012-02-23T09:40:58Z
• Authors: Marie‐Stéphanie A...; Abdelrahim Zoued; Roland Lloubès; Laure Journet; Eric Cascales
• Keywords: Cell envelope; Inner membrane; Transport protein; Peripheral membrane protein

Type VI secretion systems (T6SS) are macromolecular complexes present in Gram-negative bacteria. T6SS structurally similar to the bacteriophage cell-puncturing device and have been shown mediate bacteria-host or bacteria-bacteria interactions. assemble from 13 20 proteins. In enteroaggregative Escherichia coli (EAEC), one of subassemblies is composed four proteins that form a trans-envelope complex: TssJ outer membrane lipoprotein, peptidoglycan-anchored inner TagL protein, two putative proteins, TssL TssM. this study, we characterized protein EAEC Sci-1 terms localization, topology, function. critical component T6SS, anchored through single transmembrane segment located at extreme C-terminus protein. We further show essential for function its proper insertion dependent upon YidC modulated by Hsp70 homologue DnaK.