The interaction between "R/S domain" of rat 28S ribosomal RNA and ribosome-inactivating proteins investigated by fusidic acid.
The interaction between "R/S domain" of rat 28S rRNA and ribosome-inactivating proteins (RIPs) has been studied by blocking the action site of RIPs on "R/S domain" of 28S rRNA with fusidic acid or S100. Fusidic acid alone could form stable complexes with rat ribosomes and block the action site of RNA N-glycosidases. incubation of fusidic acid and S100 or GDP with ribosomes could also protect ribosomes from the action of ricin A-chain. However, different effect of fusidic acid, S100 an dGDP was observed when alpha-sarcin was used. Fusidic acid alone could not block the action site of alpha-sarcin. Fusidic acid together with the elongation factors in S100 could block the action site of alpha-sarcin. These results are consistent with the previous report that ricin A-chain and alpha-sarcin recognized different conformation of "R/S domain" in rat 28S rRNA.
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Shanghai Institute of Biochemistry, Academia Sinica, China.
Liu
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D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000737:chemistry*; D005672:Fusidic Acid / Q000737:chemistry; D066298:In Vitro Techniques; D008099:Liver / Q000737:chemistry* / Q000648:ultrastructure; D009699:N-Glycosyl Hydrolases / Q000037:antagonists & inhibitors; D009690:Nucleic Acid Conformation; D010940:Plant Proteins / Q000037:antagonists & inhibitors; D011500:Protein Synthesis Inhibitors / Q000737:chemistry*; D012339:RNA, Ribosomal, 28S / Q000737:chemistry*; D051381:Rats; D054788:Ribosome Inactivating Proteins; D012270:Ribosomes / Q000737:chemistry*
D000900:Anti-Bacterial Agents; D004791:Enzyme Inhibitors; D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D012339:RNA, Ribosomal, 28S; D005672:Fusidic Acid; D009699:N-Glycosyl Hydrolases; D054788:Ribosome Inactivating Proteins