Catabolism of capped (3′-5′)- and (2′-5′)-adenylates in rat liver nuclei

• Published in: FEBS letters 1984-01, Vol.166 (1), p.57-61
• Main Authors: Michels, Winfried, Schlimme, Eckhard
• Format: Article
• Language: English
• Subjects: 5′-Capped (2′-5′)-adenylate; 5′-Capped (3′-5′)-adenylate; Animals; Biological and medical sciences; Capped RNA fragment; Cell Nucleus - metabolism; Decapping activity; Fundamental and applied biological sciences. Psychology; Liver - ultrastructure; Molecular and cellular biology; Molecular genetics; Nuclear dinucleoside triphosphatase; Nucleotidases - metabolism; Phosphoric Diester Hydrolases - metabolism; Rat liver nucleus; Rats; RNA Caps - metabolism; RNA catabolism; RNA recycling; Structure-Activity Relationship; Substrate Specificity; Transcription. Transcription factor. Splicing. Rna processing
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(84)80044-7

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 3A moiety was determined in the capped RNA model compounds GP 3A3′pA, Gp 3A3′pA-isoprop and Gp 3A2′pA in isolated rat liver nuclei; i.e., in the environment in which the dinucleoside triphosphatase operates in vivo. The Gp 3A cap moiety is hydrolyzed in (3′-5′) linked nucleotides only, whereas an extension of the Gp 3A in the 2′-direction prevents the nuclear triphosphatase to operate.