Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk

LAPADULA, W; SÁNCHEZ PUERTA, M. V.; JURI AYUB, M

TOXICON

PERGAMON-ELSEVIER SCIENCE LTD

Año: 2012 vol. 59 p. 427 - 432

0041-0101

Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by depurinating an adenine on the sarcin-ricin loop (SRL) of the large subunit ribosomal RNA. Several RIPs interact with the C-terminal end of ribosomal stalk P proteins, and this interaction is required for full activity. In contrast, Pokeweed Antiviral Protein does not interact with the same component of the P proteins. Here, we provide evidence from phylogenetic analyses and sequence alignments suggesting that the interaction with the C-terminal end of P proteins evolved independently in different RIPs by convergent evolution.