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Nucleic Acids Research, 1984, Vol. 12, No. 5 2303-2315
© 1984

ENZYMOLOGY

Synthe of Gp4N and Gp3N compounds by guanylyltransferase purified from yeast

Dashou Wang* and Aaron J. Shatkin

Roche Institute of Molecular Biology, Roche Research Center Nutley, NJ 07110, USA

Received January 3, 1984. Accepted January 31, 1984.

Guanylyltransferase that catalyzes mRNA capping by the reaction, ppNpN + GTP -> GpppNpN was purified from S. cerevisiae The enzyme forms a nucleotidyl Intermediate by phosphoamide linkage of GMP. Two guanylylated polypeptides of MR ~52,000 and 46,000 were obtained, the latter apparently by proteolysis of the larger component. Both forms transferred the covalently bound GMP to ppApG, yielding GpppApG. Dinucleoside tri- and tetraphosphates of the type Gp3N and Gp4N were also produced by using ribonucleoside 5' -di and triphosphates as acceptors. The purified yeast guanylyltransferase contained little or no RNA 5'-triphosphatase or methyltransferase.

*Present address: Institute of Microbiology, Academia Sinica, Beijing, China


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