Application Notes

MST untangles the intricacy of a multimeric protein complex in its native form

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Monolith is a trademark of NanoTemper Technologies GmbH, Munich, Germany. NanoTemper is a registered trademark of NanoTemper Technologies GmbH, Munich, Germany. ©2019 NanoTemper Technologies, Inc. South San Francisco, CA, USA. All Rights Reserved. NT-MO-034 APPLICATION NOTE 4 Tumer, N. E. & Li, X. P. Interaction of ricin and Shiga toxins with ribosomes. Curr. Top. Microbiol. Immunol. 357, 1–18 (2012) 5 Chiou, J. C., Li, X. P., Remacha, M., Ballesta, J. P. & Tumer, N. E. The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae. Mol. Microbiol 70, 1441–1452 (2008) 6 McCluskey, A. J. et al. The Catalytic Subunit of Shiga-like Toxin 1 Interacts with Ribosomal Stalk Proteins and is Inhibited by Their Conserved C-Terminal Domain. J. Mol. Biol. 378, 375–386 (2008) 7 May, K. L. et al. The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells. FEBS J. 279, 3925–3936 (2012) 8 Jetzt, A. E., Li, X. P., Tumer, N. E. & Cohick, W. S. Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome. Toxicol. Appl. Pharmacol. 310, 120–128 (2016) 9 Li, X. P., Grela, P., Krokowski, D., Tchorzewski, M. & Tumer, N. E. Pentameric organization of the ribosomal stalk accelerates recruitment of ricin A chain to the ribosome for depurination. J. Biol. Chem. 285, 41463–41471 (2010) 10 Grela, P. et al. Structural properties of the human acidic ribosomal p proteins forming the p1-p2 heterocomplex. J. Biochem. 143, 169–177 (2008) 11 Tchorzewski, M., Boguszewska, A., Abramczyk, D. & Grankowski, N. Overexpression in Escherichia coli, purification, and characterization of recombinant 60S ribosomal acidic proteins from Saccharomyces cerevisiae. Protein Expr. Purif. 15, 40–47 (1999) 12 Bocharov, E. V. et al. From structure and dynamics of protein L7/L12 to molecular switching in ribosome. J. Biol. Chem. 279, 17697–17706 (2004) 13 Bernado, P. et al. Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation. Biophys. J. 98, 2374–2382 (2010) 14 Tchorzewski, M., Boguszewska, A., Dukowski, P. & Grankowski, N. Oligomerization properties of the acidic ribosomal P-proteins from Saccharomyces cerevisiae: effect of P1A protein phosphorylation on the formation of the P1A-P2B hetero-complex. Biochim. Biophys. Acta 1499, 63–73 (2000) 15 Li, X. P., Kahn, P. C., Kahn, J. N., Grela, P. & Tumer, N. E. Arginine residues on the opposite side of the active site stimulate the catalysis of ribosome depurination by ricin A chain by interacting with the P-protein stalk. J. Biol. Chem. 288, 30270–30284 (2013) 16 Lee, K. M. et al. Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex. Nucleic Acids Res. 40, 3172–3182 (2012) 17 Endo, Y., Mitsui, K., Motizuki, M. & Tsurugi, K. The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins. J. Biol. Chem. 262, 5908–5912 (1987) 18 Lord, J. M., Roberts, L. M. & Robertus, J. D. Ricin: structure, mode of action, and some current applications. FASEB J. 8, 201–208 (1994) 19 Grela, P., Li, X.P., Horbowicz, P., Dźwierzyńska, M., Tchórzewski, M. & Tumer, N.E. Human ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with aprominent role for P1 C-terminus. Scientific Reports. 7: 5608 (2017)

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