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• W2056529195 abstract "The reaction product of the ribosomal poly(A) polymerase [ATP(UTP):RNA ucleotidyltrasferase] is analyzed. Two systems are used in vitro: (a) isolated polyribosomes with endogenous enzyme and RNA primer and (b) purified enzyme with total polyribosomal RNA as primer. In the polyribosome system about 50% of the [3H]AMP label is in poly(A)-containing mRNA. This RNA displays a heterogeneous size ditribution in the range of 8–30 S with a maximum at about 14 S. Upon denaturation the maximum is shifted towards the 10–S zone. The poly(A) polymerase catalyzes the addition of 12–18 adenylate residues to pre-existing mRNA poly(A) sequences of 40–160 residues. The [3H]AMP incorporated into poly(A)-lacking RNA is mainly in a fraction with an electrophoretic mobility corresponding to 4-S RNA. In the purified enzyme system, specificity towards poly(A)-containing mRNA is lost to a considerable extent. Only 10% of the [3H]AMP label is retained by oligo(dT)-cellulose. The bulk of the product is in 18-S rRNA and heterogeneous small molecular weight RNA. We conclude that the ribosome-associated poly(A) polymerase is most likely the enzyme responsible for the cytoplasmic polyadenylation of poly(A)-containing mRNA in vivo." @default.
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• W2056529195 date "1980-01-01" @default.
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• W2056529195 title "Primer Specificity of Ribosome-Associated Poly(A) Polymerase from Ehrlich Ascites Tumour Cells" @default.
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• W2056529195 doi "https://doi.org/10.1111/j.1432-1033.1980.tb04294.x" @default.
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