Abstract
The rRNA N-glycosidase activities of the catalytically active A chains of the heterodimeric ribosome inactivating proteins (RIPs) ricin and abrin, the single-chain RIPs dianthin 30, dianthin 32, and the leaf and seed forms of pokeweed antiviral protein (PAP) were assayed on E. coli ribosomes. All of the single-chain RIPs were active on E. coli ribosomes as judged by the release of a 243 nucleotide fragment from the 3' end of 23S rRNA following aniline treatment of the RNA. In contrast, E. coli ribosomes were refractory to the A chains of ricin and abrin. The position of the modification of 23S rRNA by dianthin 32 was determined by primer extension and found to be A2660, which lies in a sequence that is highly conserved in all species.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Abrin / chemistry
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Amino Acid Sequence
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Apurinic Acid / chemistry
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Base Sequence
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Binding Sites
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Escherichia coli / ultrastructure
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Molecular Sequence Data
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N-Glycosyl Hydrolases*
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Plant Proteins / pharmacology*
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Protein Synthesis Inhibitors / pharmacology*
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RNA, Bacterial / chemistry
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RNA, Ribosomal / chemistry
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RNA, Ribosomal, 23S / chemistry*
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Ribosome Inactivating Proteins, Type 1
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Ricin / chemistry
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Structure-Activity Relationship
Substances
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Plant Proteins
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Protein Synthesis Inhibitors
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RNA, Bacterial
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RNA, Ribosomal
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RNA, Ribosomal, 23S
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RNA, ribosomal, 26S
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Ribosome Inactivating Proteins, Type 1
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Apurinic Acid
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Abrin
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Ricin
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N-Glycosyl Hydrolases
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MAP protein, Mirabilis jalapa
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pokeweed antiviral protein