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

Authors :
Julien Stathopulos
Abdelrahim Zoued
Christine Kellenberger
Maxence S. Vincent
Alain Roussel
Philippe Leone
Mickaël J. Canestrari
Christian Cambillau
Eric Cascales
Bérengère Ize
Laboratoire d'ingénierie des systèmes macromoléculaires (LISM)
Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU)
Architecture et fonction des macromolécules biologiques (AFMB)
Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)
Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)
Source :
Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2017, 292 (8), pp.3252-3261. ⟨10.1074/jbc.M116.765081⟩, Journal of Biological Chemistry, 2017, 292 (8), pp.3252-3261. ⟨10.1074/jbc.M116.765081⟩
Publication Year :
2017
Publisher :
HAL CCSD, 2017.

Abstract

International audience; The transport of proteins at the cell surface of Bacteriodetes 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 Flavobacteria, S-layer components in Tannerella forsythia and tooth tissue-degrading enzymes in the oral pathogen Porphyromonas gingivalis. While 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.

Details

Language :
English
ISSN :
00219258 and 1083351X
Database :
OpenAIRE
Journal :
Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2017, 292 (8), pp.3252-3261. ⟨10.1074/jbc.M116.765081⟩, Journal of Biological Chemistry, 2017, 292 (8), pp.3252-3261. ⟨10.1074/jbc.M116.765081⟩
Accession number :
edsair.doi.dedup.....4aa763acb956986506fec4589c905986