Phosphorylation of the conserved C?terminal domain of ribosomal P?proteins impairs the mode of interaction with plant toxins

The ribosome is subjected to post-translational modifications, including phosphorylation, that affect its biological activity. Among ribosomal elements, the P-proteins undergo phosphorylation within C terminus, element which interacts with trGTPases or ribosome-inactivating proteins (RIPs); however, role of has never been elucidated. Here, we probed function on interaction RIPs using P1-P2 dimer. We determined kinetic parameters toxins biolayer interferometry and microscale thermophoresis. results present first mechanistic insight into P-protein showing introduction a negative charge terminus promotes ?-helix formation decreases affinity for RIPs.