RNA polymerase of influenza virus. IV. Catalytic properties of the capped RNA endonuclease associated with the RNA polymerase.
Catalytic properties of the capped RNA-specific endonuclease associated with the influenza virus RNA polymerase were analyzed with use of synthetic hetero- and homopolymers containing 32P-labeled CAP structures at their 5' termini. The endonuclease displays its intrinsic activity provided that substrate RNA contains both the CAP-1 structure (m7GpppGm) and either A or U residues at 9 to 11 nucleotides distant from the CAP structure. Independent recognition of multiple RNA signals by the endonuclease was further supported by the findings that dinucleotide ApG, free CAP structures and RNA without the CAP structure inhibited the endonuclease activity to different extents. In the presence of four species of ribonucleoside 5'-triphosphates, the endonucleolytically cleaved fragments with the CAP-1 structure were incorporated into polynucleotides, supporting the concept that they are used as the primers for the transcription. The initial nucleotide linked to the primers was a G residue, the nucleotide complementary to the second base of the 3' termini of the vRNA segments.
D000818:Animals; D001483:Base Sequence; D002642:Chick Embryo; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004722:Endoribonucleases / Q000378:metabolism*; D009980:Influenza A virus / Q000201:enzymology*; D007700:Kinetics; D012315:RNA Caps; D013379:Substrate Specificity
D012315:RNA Caps; D012321:DNA-Directed RNA Polymerases; D004722:Endoribonucleases