Dissection of the TssB-TssC interface during type VI secretion sheath complex formation

• Published in: PloS one Vol. 8; no. 11; p. e81074
• Main Authors: Zhang, Xiang Y, Brunet, Yannick R, Logger, Laureen, Douzi, Badreddine, Cambillau, Christian, Journet, Laure, Cascales, Eric
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 25.11.2013; Public Library of Science (PLoS)
• Subjects: Bacteria; Bacteriophages - metabolism; Biochemistry; Biochemistry, Molecular Biology; Biophysics; Burkholderia cenocepacia; Cloning; Complex formation; Contractility; Contraction; Delivery contracts; Dissection; DNA methylation; E coli; Elongation; Escherichia coli; Fluorescence; Fluorescence microscopy; Francisella tularensis; Genes; HCP protein; Hydrophobicity; Life Sciences; Microscopy, Fluorescence; Molecular biology; Mutagenesis; Mutagenesis, Site-Directed; Phages; Proteins; Secretion; Signal transduction; Site-directed mutagenesis; Structural Biology; Toxins; Vibrio cholerae; Viral Proteins - genetics; Viral Proteins - metabolism; Yersinia pseudotuberculosis; France; Bacteriophages; Vibrio cholerae; Pseudomonas aeruginosa; Substitution mutation; Protein interactions; Protein structure; Fluorescence microscopy; Secretion systems

The Type VI secretion system (T6SS) is a versatile machine that delivers toxins into either eukaryotic or bacterial cells. At a molecular level, the T6SS is composed of a membrane complex that anchors a long cytoplasmic tubular structure to the cell envelope. This structure is thought to resemble th...