PXD038000

PXD038000 is an original dataset announced via ProteomeXchange.

Title	Moonlighting chaperone 1 activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa
Description	Pseudomonas aeruginosa 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 P. aeruginosa, with the rhl circuit playing the leading role in late and chronic infections. The majority of traits controlled by rhl transcription factor RhlR depend on PqsE, a dispensable thioesterase in Pseudomonas 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 N-butanoyl-L-homoserine lactone (C4-HSL), solubilizes RhlR and thereby renders the otherwise insoluble transcription factor active. We determined crystal structures of the complex and identified residues essential for the interaction. To corroborate the chaperone like activity of PqsE, we designed stability-optimized variants of RhlR that bypass the need for C4-HSL and PqsE in activating PqsE/RhlR-controlled processes of P. aeruginosa. Together, our data provide insight into the unique regulatory role of PqsE and lay groundwork for developing new P. aeruginosa-specific pharmaceuticals.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:42:45.052.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Lothar Jaensch
SpeciesList	scientific name: Pseudomonas aeruginosa PA14; NCBI TaxID: 652611;
ModificationList	iodoacetamide derivatized residue
Instrument	timsTOF Pro; LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2022-11-07 09:43:14	ID requested
1	2023-03-11 04:03:19	announced
⏵ 2	2023-11-14 08:42:53	announced	2023-11-14: Updated project metadata.

Borgert SR, Henke S, Witzgall F, Schmelz S, Zur Lage S, Hotop SK, Stephen S, L, ü, bken D, Kr, ü, ger J, Gomez NO, van Ham M, J, ä, nsch L, Kalesse M, Pich A, Br, ö, nstrup M, H, ä, ussler S, Blankenfeldt W, Moonlighting chaperone activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa. Nat Commun, 13(1):7402(2022) [pubmed]

submitter keyword: RhlR,Pseudomonas aeruginosa, PqsE, quorum sensing, LC-MS/MS

Lothar Jänsch, Wulf Blankenfeldt
contact affiliation	Department Structure and Function of Proteins Helmholtz Centre for Infection Research Inhoffenstr. 7, 38124 Braunschweig, Germany
contact email	lothar.jaensch@helmholtz-hzi.de
lab head
Lothar Jaensch
contact affiliation	HZI
contact email	Lothar.Jaensch@Helmholtz-HZI.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/03/PXD038000

PRIDE project URI

• PRIDE
  1. PXD038000
     1. Label: PRIDE project
     2. Name: Moonlighting chaperone 1 activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa