Abstract: All bacteria compete for growth niches and other limited resources in the environment. These existential battles are waged at several levels, but one common strategy entails the direct transfer of toxic effector proteins between competing cells. Antibacterial effectors are invariably encoded with cognate immunity proteins, which protect the cell from intoxication by neighboring siblings. Here, I show that an immunity protein from Enterobacter cloacae is also required to activate its cognate phospholipase effector prior to delivery into target bacteria. Genetic, biochemical and structural analyses reveal that the phospholipase effector is subject to a novel post-translational modification when bound to its immunity protein. This modification stabilizes the fold of the phospholipase and is absolutely required for its enzymatic activity in vitro and in vivo. Join us to learn the identity of this new post-translational modificatio
Student Host: Adrika Raybarman – Govindjee Award for Excellence in Biological Research Fellow
