| Literature DB >> 28057754 |
Maxence S Vincent1, Mickaël J Canestrari1, Philippe Leone2, Julien Stathopulos2, Bérengère Ize1, Abdelrahim Zoued1, Christian Cambillau2, Christine Kellenberger2, Alain Roussel2, Eric Cascales3.
Abstract
The transport of proteins at the cell surface of Bacteroidetes depends on a secretory apparatus known as type IX secretion system (T9SS). This machine is responsible for the cell surface exposition of various proteins, such as adhesins, required for gliding motility in Flavobacterium, S-layer components in Tannerella forsythia, and tooth tissue-degrading enzymes in the oral pathogen Porphyromonas gingivalis Although a number of subunits of the T9SS have been identified, we lack details on the architecture of this secretion apparatus. Here we provide evidence that five of the genes encoding the core complex of the T9SS are co-transcribed and that the gene products are distributed in the cell envelope. Protein-protein interaction studies then revealed that these proteins oligomerize and interact through a dense network of contacts.Entities:
Keywords: bacterial pathogenesis; membrane protein; microbiology; protein assembly; protein complex; protein purification; protein secretion; secretion
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Year: 2017 PMID: 28057754 PMCID: PMC5336160 DOI: 10.1074/jbc.M116.765081
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157