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The PqsE Protein Interaction Network in Pseudomonas aeruginosa

ABSTRACT: The PqsE enzyme plays a vital role in quorum sensing and virulence in Pseudomonas aeruginosa, yet its enzymatic function is unknown. Here, we identify the protein interaction network of PqsE as well as that of a catalytically dead variant, PqsE(D73A) in P. aeruginosa PA14. Our analyses identify proteins that interact with PqsE that are independent of and that depend on PqsE catalytic function. One such catalysis-independent interaction is with the quorum-sensing regulator, RhlR, consistent with our previous work. We also characterize the PqsE interaction network in a delta rhlR P. aeruginosa PA14 strain and identify additional proteins as PqsE-interactors.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Pseudomonas Sp. Bacteria

SUBMITTER: Todd Greco

LAB HEAD: Ileana M Cristea

PROVIDER: PXD035779 | Pride | 2022-09-06

REPOSITORIES: Pride

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Protein Interaction Networks of Catalytically Active and Catalytically Inactive PqsE in Pseudomonas aeruginosa.

Taylor Isabelle R IR Murray-Nerger Laura A LA Greco Todd M TM Liu Dawei D Cristea Ileana M IM Bassler Bonnie L BL

mBio 20220908 5

Pseudomonas aeruginosa is a human pathogen that relies on quorum sensing to establish infections. The PqsE quorum-sensing protein is required for P. aeruginosa virulence factor production and infection. PqsE has a reported enzymatic function in the biosynthesis of the quorum-sensing autoinducer called PQS. However, this activity is redundant because, in the absence of PqsE, this role is fulfilled by alternative thioesterases. Rather, PqsE drives P. aeruginosa pathogenic traits via a protein-prot ...[more]

PMID: 36073810

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