Modulation of Rab GTPase function by a protein phosphocholine transferase

摘要

The intracellular pathogen Legionella pneumophila modulates the activity of host GTPases to direct the transport and assembly of the membrane-bound compartment in which it resides. In vitro studies have indicated that the Legionella protein DrrA post-translationally modifies the GTPase Rabl by a process called AMPylation. Here we used mass spectrometry to investigate post-translational modifications to Rabl that occur during infection of host cells by Legionella. Consistent with in vitro studies, DrrA-mediated AMPylation of a conserved tyrosine residue in the switch II region of Rabl was detected during infection.