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. 1973 Dec;70(12 Pt 1-2):3400–3404. doi: 10.1073/pnas.70.12.3400

Reticulocyte RNA-Dependent RNA Polymerase

Kathleen M Downey 1, John J Byrnes 1, Bonnie S Jurmark 1, Antero G So 1
PMCID: PMC427245  PMID: 4519633

Abstract

A cytoplasmic, microsomal bound RNA-dependent RNA polymerase has been purified 2500-fold from rabbit reticulocyte lysates. The synthesis of RNA with the purified enzyme is absolutely dependent on the addition of an RNA template. The best template is hemoglobin messenger RNA, while bacteriophage RNA and poly(A,G) are less active, and DNA is completely inactive as a template. With poly(A,G) as a template, only UTP and CTP are incorporated into polynucleotide chains, indicating that the RNA polymerase is an RNA replicase and not a terminal transferase. With messenger RNA as a template, all four ribonucleoside triphosphates are required for maximal activity. The RNA-dependent RNA polymerase reaction is extremely sensitive to low concentrations of heme, rifamycin AF/013, and ribonuclease and resistant to actinomycin D and DNase. The discovery of RNA-directed RNA synthesis in reticulocytes offers an additional site for control of gene expression in mammalian cells and provides a possible mechanism for amplification of the expression of specific genes.

Keywords: RNA replicase, hemoglobin mRNA, heme

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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