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Borgert, Sebastian Roman; Henke, Steffi; Witzgall, Florian; Schmelz, Stefan; zur Lage, Susanne; Hotop, Sven-Kevin; Stephen, Steffi; Lübken, Dennis; Krüger, Jonas; Gomez, Nicolas Oswaldo; van Ham, Marco; Jänsch, Lothar; Kalesse, Markus; Pich, Andreas; Brönstrup, Mark; Häussler, Susanne; Blankenfeldt, Wulf

Moonlighting chaperone activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa

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  • Medientyp: E-Artikel
  • Titel: Moonlighting chaperone activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa
  • Beteiligte: Borgert, Sebastian Roman; Henke, Steffi; Witzgall, Florian; Schmelz, Stefan; zur Lage, Susanne; Hotop, Sven-Kevin; Stephen, Steffi; Lübken, Dennis; Krüger, Jonas; Gomez, Nicolas Oswaldo; van Ham, Marco; Jänsch, Lothar; Kalesse, Markus; Pich, Andreas; Brönstrup, Mark; Häussler, Susanne; Blankenfeldt, Wulf
  • Erschienen: Springer Science and Business Media LLC, 2022
  • Erschienen in: Nature Communications, 13 (2022) 1
  • Sprache: Englisch
  • DOI: 10.1038/s41467-022-35030-w
  • ISSN: 2041-1723
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: <jats:title>Abstract</jats:title><jats:p><jats:italic>Pseudomonas aeruginosa</jats:italic> is a major cause of nosocomial infections and also leads to severe exacerbations in cystic fibrosis or chronic obstructive pulmonary disease. Three intertwined quorum sensing systems control virulence of <jats:italic>P. aeruginosa</jats:italic>, with the <jats:italic>rhl</jats:italic> circuit playing the leading role in late and chronic infections. The majority of traits controlled by <jats:italic>rhl</jats:italic> transcription factor RhlR depend on PqsE, a dispensable thioesterase in <jats:italic>Pseudomonas</jats:italic> Quinolone Signal (PQS) biosynthesis that interferes with RhlR through an enigmatic mechanism likely involving direct interaction of both proteins. Here we show that PqsE and RhlR form a 2:2 protein complex that, together with RhlR agonist <jats:italic>N</jats:italic>-butanoyl-L-homoserine lactone (C4-HSL), solubilizes RhlR and thereby renders the otherwise insoluble transcription factor active. We determine crystal structures of the complex and identify residues essential for the interaction. To corroborate the chaperone-like activity of PqsE, we design stability-optimized variants of RhlR that bypass the need for C4-HSL and PqsE in activating PqsE/RhlR-controlled processes of <jats:italic>P. aeruginosa</jats:italic>. Together, our data provide insight into the unique regulatory role of PqsE and lay groundwork for developing new <jats:italic>P. aeruginosa</jats:italic>-specific pharmaceuticals.</jats:p>
  • Zugangsstatus: Freier Zugang