Open AccessSynthe of Gp4N and Gp3N compounds by guanylyltransferase purified from yeast
Author(s) -
Dashou Wang,
Aaron J. Shatkin
Publication year - 1984
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/12.5.2303
Subject(s) - biology , biochemistry , triphosphatase , gtp' , enzyme , ribonucleoside , yeast , saccharomyces cerevisiae , rna , proteolysis , microbiology and biotechnology , dna , gene
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 approximately 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.