Mechanism and function of protein glutamylation during Legionella infection – BACTGLU
Legionella pneumophila secretes ~300 effector proteins into the host cytosol during infection. These effectors exert multitude of biochemical activities and drive the maturation of Legionella containing vacuole (LCV) by hijacking several host defense pathways. Deletion of the effector SidJ negatively impacts legionella’s intra cellular growth. We recently showed that SidJ acts as a glutamylating enzyme that adopts a novel fold with distant similarity to kinase domains. SidJ shows no sequence or structural homology to mammalian glutamylating enzymes and contains two nucleotide-binding pockets. My proposal aims to address how SidJ recognizes its target proteins for glutamylation, how the two ATP-bindings pockets of SidJ co-ordinate to achieve target protein glutamylation and what host proteins does SidJ target especially after early stages of legionella infection.
Project coordination
Sagar Bhogaraju (European Molecular Biology Laboratory)
The author of this summary is the project coordinator, who is responsible for the content of this summary. The ANR declines any responsibility as for its contents.
Partner
EMBL European Molecular Biology Laboratory
Help of the ANR 274,963 euros
Beginning and duration of the scientific project:
October 2021
- 36 Months