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The site of action of the A‐chain of mistletoe lectin I on eukaryotic ribosomes The RNA N ‐glycosidase activity of the protein
Author(s) -
Endo Yaeta,
Tsurugi Kunio,
Franz Hartmut
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80853-6
Subject(s) - ribosome inactivating protein , ribosome , lectin , ricin , rna , chemistry , protein biosynthesis , biochemistry , translation (biology) , microbiology and biotechnology , biology , messenger rna , gene , toxin
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.