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The C-terminal end of P proteins mediates ribosome inactivation by trichosanthin but does not affect the pokeweed antiviral protein activity |
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| Authors: | Ayub Maximiliano Juri Smulski Cristian R Ma Kit-Wan Levin Mariano J Shaw Pang-Chui Wong Kam-Bo |
| Institution: | a Fundación Instituto Leloir, IIBBA-CONICET and University of Buenos Aires, Patricias Argentinas 435, 1405 Buenos Aires, Argentina b Centre for Protein Science and Crystallography, Department of Biochemistry, The Chinese University of Hong Kong, Hong Kong, China c Laboratorio de Biología Molecular de la Enfermedad de Chagas (LaBMECh), Instituto de Investigaciones en Ingeniería Genética y Biología Molecular (INGEBI-CONICET), Buenos Aires, Argentina d Department of Maladies Infectieuses (U.INSERM 567)-Institut Cochin, Paris, France |
| Abstract: | Ribosome inactivating proteins (RIPs) inhibit protein synthesis depurinating a conserved residue in the sarcin/ricin loop of ribosomes. Some RIPs are only active against eukaryotic ribosomes, but other RIPs inactivate with similar efficiency prokaryotic and eukaryotic ribosomes, suggesting that different RIPs would interact with different proteins. The SRL in Trypanosoma cruzi ribosomes is located on a 178b RNA molecule named 28Sδ. In addition, T. cruzi ribosomes are remarkably resistant to TCS. In spite of these peculiarities, we show that TCS specifically depurinate the predicted A51 residue on 28Sδ. We also demonstrated that the C-terminal end of ribosomal P proteins is needed for full activity of the toxin. In contrast to TCS, PAP inactivated efficiently T.cruzi ribosomes, and most importantly, does not require from the C-terminal end of P proteins. These results could explain, at least partially, the different selectivity of these toxins against prokaryotic and eukaryotic ribosomes. |
| Keywords: | Trypanosoma Protein synthesis Trichosanthin Pokeweed antiviral protein Ribosome inactivating protein (RIP) |
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