Catabolism of capped (3'-5')- and (2'-5')-adenylates in rat liver nuclei.
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 Gp3A moiety was determined in the capped RNA model compounds Gp3A3'pA, Gp3A3'pA-isoprop and Gp3A2'pA in isolated rat liver nuclei; i.e., in the environment in which the dinucleoside triphosphatase operates in vivo. The Gp3A cap moiety is hydrolyzed in (3'-5') linked nucleotides only, whereas an extension of the Gp3A in the 2'-direction prevents the nuclear triphosphatase to operate.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D008099:Liver / Q000648:ultrastructure; D009708:Nucleotidases / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D012315:RNA Caps / Q000378:metabolism*; D051381:Rats; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D012315:RNA Caps; D009708:Nucleotidases; D010727:Phosphoric Diester Hydrolases