4.6 Article

Characterization of the Porphyromonas gingivalis Type IX Secretion Trans-envelope PorKLMNP Core Complex

Journal

JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 292, Issue 8, Pages 3252-3261

Publisher

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M116.765081

Keywords

bacterial pathogenesis; membrane protein; microbiology; protein assembly; protein complex; protein purification; protein secretion; secretion

Funding

  1. CNRS
  2. Aix-Marseille Universite
  3. Agence Nationale de la Recherche [ANR-15-CE11-0019-01]
  4. French Ministere de la Recherche
  5. Fondation pour la Recherche Medicale [FDT20140931060]
  6. Agence Nationale de la Recherche (ANR) [ANR-15-CE11-0019] Funding Source: Agence Nationale de la Recherche (ANR)

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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.

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