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Degradation by the 2',5'‐phosphodiesterase activity of mouse cells requires the presence of a ribo hydroxyl group in the penultimate position of the oligonucleotide substrate
Author(s) -
Torrence Paul F.,
Alster David,
Huss Sophie,
Gosselin Gilles,
Imbach Jean-Louis
Publication year - 1987
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(87)81358-3
Subject(s) - tetramer , phosphodiesterase , trimer , oligonucleotide , chemistry , stereochemistry , nucleotide , residue (chemistry) , substrate (aquarium) , biochemistry , enzyme , dimer , biology , dna , organic chemistry , ecology , gene
A series of 9‐β‐D‐xylofuranosyladenine (xyloA or xyloadenosine) substituted analogs of 2‐5A core trimer and tetramer were examined for their ability to be degraded by the 2',5'‐phosphodiesterase activity of cytoplasmic extracts of mouse L cells. Two distinct groups of xyloA‐substituted analogs could be readily discriminated. The first group contained xyloadenosine at the 2'‐termini and included A2'p5'A2'p5'(xyloA) and A2'p5'A2/p5'A2'p5'(xyloA). These oligomers behaved as did their parent oligoadenylates in that they were equally sensitive to degradation by the 2',5'‐phosphodiesterase activity. The second group of oligonucleotides bore a xyloadenosine residue in the penultimate nucleotide residues of the oligomers and included A2'p5'(xyloA)2'p5'(xyloA), (xyloA)2'p5'(xyloA)2'p5'(xyloA), A2'p5'A2'p5'(xyloA)2'p5'(xyloA) and (xyloA)2'p5' (xyloA)2'p5'(xyloA)2'p5'(xyloA). This group was quite resistant to 2',5'‐phosphodiesterase activity. In all, the findings demonstrate that the ribo configuration 3'‐hydroxyl group in the penultimate nucleotide of the oligonucleotide substrate is a prerequisite for the 2',5'‐phosphodiesterase activity.