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Nucleic Acids Research, 1983, Vol. 11, No. 11 3637-3649
© 1983

ENZYMOLOGY

RNA polymerase of influenza virus. IV. Catalytic properties of the capped RNA endonuclease associated with the RNA polymerase

Kiyoshi Kawakami1, Kiyohisa Mizumoto2 and Akira Ishihama*,1

1Department of Biochemistry, Institute for Virus Research, Kyoto University Kyoto 606, Japan 2Department of Biochemistry, Institute of Medical Science, University of Tokyo Tokyo 108, Japan

*To whom reprint requests should be addressed

Received March 14, 1983. Revised May 2, 1983. Accepted May 9, 1983.

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 dlnucleotide 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 incorpo* rated 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.


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