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• W38861811 abstract "Research Article1 January 1989free access Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides. M. J. May M. J. May Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author M. R. Hartley M. R. Hartley Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author L. M. Roberts L. M. Roberts Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author P. A. Krieg P. A. Krieg Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author R. W. Osborn R. W. Osborn Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author J. M. Lord J. M. Lord Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author M. J. May M. J. May Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author M. R. Hartley M. R. Hartley Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author L. M. Roberts L. M. Roberts Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author P. A. Krieg P. A. Krieg Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author R. W. Osborn R. W. Osborn Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author J. M. Lord J. M. Lord Department of Biological Sciences, University of Warwick, Coventry, UK. Search for more papers by this author Author Information M. J. May1, M. R. Hartley1, L. M. Roberts1, P. A. Krieg1, R. W. Osborn1 and J. M. Lord1 1Department of Biological Sciences, University of Warwick, Coventry, UK. The EMBO Journal (1989)8:301-308https://doi.org/10.1002/j.1460-2075.1989.tb03377.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info When recombinant ricin A chain transcripts are translated in a rabbit reticulocyte lysate the ribosomes are rapidly inactivated as shown by their inability to support translation of yeast preproalpha factor or chicken lysozyme transcripts added subsequently. In contrast, ribosomes which have translated transcripts encoding non-toxic polypeptides such as ricin B chain, readily translate the second transcript under identical conditions. Ribosome inactivation is accompanied by a highly specific modification of 28S rRNA which occurs at the same position as the N-glycosidic cleavage of an adenine residue and which is thought to cause inactivation of the ribosomes. Protein synthesis by wheat germ ribosomes was not inhibited under the conditions which inhibit reticulocyte ribosomes confirming earlier observations that plant cytoplasmic ribosomes are much less sensitive to inhibition by ricin A chain than are mammalian ribosomes. Using the same assay we have shown that deleting an internal hexapeptide, which shares homology with hamster elongation factor-2, completely abolishes catalytic activity. Deleting a second pentapeptide conserved between ricin A chain and the ribosome-inactivating plant toxin trichosanthin, had no effect. Deleting the first nine residues from the N-terminus of A chain did not affect toxicity whereas deleting a further three residues inactivated the polypeptide. Point mutations which individually converted arginine 48 and arginine 56 of ricin A chain to alanine residues or which deleted arginine 56 were also without effect on the catalytic activity of the toxin. Previous ArticleNext Article Volume 8Issue 11 January 1989In this issue RelatedDetailsLoading ..." @default.
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• W38861811 title "Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides." @default.
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