Related Experiment Video
Updated: Apr 27, 2026

Replication of the Ordered, Nonredundant Library of Pseudomonas aeruginosa strain PA14 Transposon Insertion Mutants
Published on: May 4, 2018
Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas aeruginosa PA14 strain
Tassadit Ouidir1, Frédérique Jarnier, Pascal Cosette
1Polymers, Biopolymers, Surfaces Laboratory, CNRS, UMR 6270, Mont-Saint-Aignan, France; Normandie University, UR, Mont-Saint-Aignan, France; PISSARO Proteomic Platform, Institute for Research and Innovation in Biomedicine, University of Rouen, Mont Saint Aignan, France.
Abstract:
Protein phosphorylation on serine, threonine, and tyrosine is known to be involved in a wide variety of cellular processes, signal transduction, and bacterial virulence. We characterized, for the first time, the extracellular phosphoproteins of the Pseudomonas aeruginosa PA14 strain. We identified 28 phosphoproteins (59 phosphosites) including enzymes, with various phosphorylation sites, known as potent secreted virulence factors in P. aeruginosa. The high phosphorylation level of these virulence factors might reflect a relationship between Ser/Thr/Tyr phosphorylation and virulence.
More Related Videos
Related Concept Videos
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Atypical Pneumonia
Tail-anchoring of Proteins in the ER Membrane
Bacterial Translocation and Protein Secretion

