Abstract
Ribosome-inactivating proteins, such as ricin, pepocin and gypsophilin, catalyze the hydrolysis of a single N-glycosidic bond at a specific position in rRNAs. Aptamers targeting pepocin were selected from a random sequence RNA pool that spanned 30 positions. After 8 rounds, the anti-pepocin aptamers were sequenced and a conserved hairpin motif was identified. Interestingly, the selected motif is quite different from the toxin-binding domains of rRNAs.
MeSH terms
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Base Sequence
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Binding Sites
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Hydrolysis
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Ligands
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Nucleic Acid Conformation
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Oligoribonucleotides / chemistry*
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Plant Proteins / chemistry*
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Plant Proteins / pharmacology
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RNA, Ribosomal / chemistry*
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Ribosome Inactivating Proteins, Type 1
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Ribosomes / drug effects*
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Ribosomes / metabolism
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Ricin / chemistry*
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Ricin / pharmacology
Substances
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Ligands
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Oligoribonucleotides
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Plant Proteins
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RNA, Ribosomal
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Ribosome Inactivating Proteins, Type 1
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gypsophilin protein, Gypsophila elegans
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pepocin protein, Cucurbita pepo
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Ricin