Structure and specificity of the Type VI secretion system ClpV-TssC interaction in enteroaggregative Escherichia coli

• DOI: 10.1038/srep34405
• Publication Date: 2016-10-04T11:22:28Z
• Authors: Badreddine Douzi; Yannick R. Brunet; Silvia Spinelli; Valentine Lensi; Pierre Legrand; Stéphanie Blangy; Anant Kumar; Laure Journet; Eric Cascales; Christian Cambillau
• Keywords: Cell envelope

Abstract The Type VI secretion system (T6SS) is a versatile machine that delivers toxins into either eukaryotic or bacterial cells. It thus represents key player in pathogenesis and inter-bacterial competition. Schematically, the T6SS can be viewed as contractile tail structure anchored to cell envelope. contraction of sheath propels inner tube loaded with effectors towards target cell. components contracted are then recycled by ClpV AAA + ATPase for new cycle elongation. widespread Gram-negative bacteria most their genomes carry several copies gene clusters, which might activated different conditions. Here, we show ATPases encoded within two clusters enteroaggregative Escherichia coli not interchangeable specifically participate activity cognate T6SS. Here this specificity dictated interaction between N-terminal domains helices TssC1 proteins. We also present crystal ClpV1 domain, alone complex peptide, highlighting commonalities diversities recruitment sheaths.