Ribonuclease activity associated with the 60S ribosome-inactivating proteins ricin A, phytolaccin and Shiga toxin.
All purified preparations of the ribosome-inactivating proteins ricin A, phytolaccin and Shiga toxin were shown to exhibit ribonuclease activity with 5S or 5.8S rRNA substrates. These toxin species generated reproducible patterns of RNA fragments distinct for each toxin species while multiple preparations of a single toxin species yielded similar RNA fragment patterns. The heat inactivation profile of Shiga toxin was identical for its RNase and protein synthesis inhibitory activities. These data are the first to indicate that the ribosome-inactivating catalytic toxins, in addition to alpha-sarcin, exhibit RNase activity. These results suggest RNase activity may be responsible for ribosome-inactivation catalyzed by ricin, phytolaccin and Shiga toxin proteins.
D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006868:Hydrolysis; D037121:Plant Lectins; D010940:Plant Proteins / Q000378:metabolism*; D010947:Plants, Toxic; D014176:Protein Biosynthesis / Q000187:drug effects; D011489:Protein Denaturation; D012335:RNA, Ribosomal / Q000378:metabolism; D011817:Rabbits; D012260:Ribonucleases / Q000378:metabolism*; D054790:Ribosome Inactivating Proteins, Type 2; D012276:Ricin / Q000378:metabolism*; D022603:Shiga Toxins
D001427:Bacterial Toxins; D037121:Plant Lectins; D010940:Plant Proteins; D012335:RNA, Ribosomal; D054790:Ribosome Inactivating Proteins, Type 2; D022603:Shiga Toxins; C046253:phytolaccin protein, Phytolacca americana; D012276:Ricin; D012260:Ribonucleases