In vitro selection of aptamers that bind to ribosome-inactivating toxins.
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.
Hirao
I
I
Yokoyama CytoLogic Project, ERATO, Saitama, Japan.
Yoshinari
S
S
Yokoyama
S
S
Endo
Y
Y
Ellington
A D
AD
D001483:Base Sequence; D001665:Binding Sites; D006868:Hydrolysis; D008024:Ligands; D009690:Nucleic Acid Conformation; D009843:Oligoribonucleotides / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry* / Q000494:pharmacology; D012335:RNA, Ribosomal / Q000737:chemistry*; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000187:drug effects* / Q000378:metabolism; D012276:Ricin / Q000737:chemistry* / Q000494:pharmacology
D008024:Ligands; D009843:Oligoribonucleotides; D010940:Plant Proteins; D012335:RNA, Ribosomal; D054789:Ribosome Inactivating Proteins, Type 1; C105046:gypsophilin protein, Gypsophila elegans; C113092:pepocin protein, Cucurbita pepo; D012276:Ricin