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Catabolism of capped (3′‐5′)‐ and (2′‐5′)‐adenylates in rat liver nuclei
Author(s) -
Michels Winfried,
Schlimme Eckhard
Publication year - 1984
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(84)80044-7
Subject(s) - moiety , catabolism , triphosphatase , enzyme , biochemistry , adenosine triphosphatase , chemistry , rna , in vivo , hydrolysis , nucleotide , stereochemistry , biology , atpase , microbiology and biotechnology , gene
We describe studies concerning the ability of a nuclear dinucleoside triphosphatase to act as a decapping enzyme in RNA catabolism. The enzymatic release of GMP from the Gp 3 A moiety was determined in the capped RNA model compounds GP 3 A3′pA, Gp 3 A3′pA‐isoprop and Gp 3 A2′pA in isolated rat liver nuclei; i.e., in the environment in which the dinucleoside triphosphatase operates in vivo. The Gp 3 A cap moiety is hydrolyzed in (3′‐5′) linked nucleotides only, whereas an extension of the Gp 3 A in the 2′‐direction prevents the nuclear triphosphatase to operate.