The site of action of the A-chain of mistletoe lectin I on eukaryotic ribosomes. The RNA N-glycosidase activity of the protein.
The site of action of the A-chain of mistletoe lectin (ML-A) from Viscum album on eukaryotic ribosomes was studied. Treatment of rat liver ribosomes with ML-A, followed by treatment of the isolated rRNA with aniline, caused the release of a fragment with about 450 nucleotides from 28 S rRNA. Further analysis of nucleotide sequences of this fragment revealed that the aniline-sensitive site of phosphodiester bond was between positions A-4324 and G-4325 in 28 S rRNA. These results indicate that ML-A inactivates the ribosomes by cleaving a N-glycosidic bond at A-4324 of 28 S rRNA in the ribosomes as ricin A-chain does.
Endo
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Department of Biochemistry, Yamanashi Medical College, Japan.
Tsurugi
K
K
Franz
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H
D000818:Animals; D001483:Base Sequence; D008099:Liver / Q000032:analysis; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D028321:Plant Preparations; D010940:Plant Proteins; D012335:RNA, Ribosomal / Q000187:drug effects*; D012339:RNA, Ribosomal, 28S / Q000187:drug effects* / Q000378:metabolism; D051381:Rats; D054788:Ribosome Inactivating Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D012270:Ribosomes / Q000187:drug effects* / Q000378:metabolism; D014118:Toxins, Biological / Q000378:metabolism / Q000494:pharmacology*
D028321:Plant Preparations; D010940:Plant Proteins; D012335:RNA, Ribosomal; D012339:RNA, Ribosomal, 28S; D054790:Ribosome Inactivating Proteins, Type 2; D014118:Toxins, Biological; C009674:ribosome inactivating protein, Viscum; D009699:N-Glycosyl Hydrolases; D054788:Ribosome Inactivating Proteins