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Dependence of depurination of oligoribonucleotides by ricin A‐chain on divalent cations and chelating agents
Author(s) -
Glück Anton,
Wool Ira G.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201301
Subject(s) - ricin , depurination , ribosome , divalent , ribosome inactivating protein , chemistry , chelation , biochemistry , rna , stereochemistry , dna , organic chemistry , toxin , gene
Ricin A‐chain is a cytotoxic RNA N‐glycosidase that inactivates eukaryotic ribosomes by depurinating the adenosine at position 4324 in 28S rRNA. The enzyme retains its specificity when a synthetic oligoribonucleotide (a 35‐mer) that mimics the structure at the site of action is the substrate. However, covalent modification by ricin A‐chain of the oligoribonucleotide but not of ribosomes, depends on the simultaneous presence of a divalent cation and a chelating agent.