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.
| Original language | English |
|---|---|
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 70 |
| Issue number | 12 |
| State | Published - Dec 1 1973 |
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ASJC Scopus subject areas
- General
- Genetics
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Reticulocyte RNA dependent RNA polymerase. / Downey, K. M.; Byrnes, John; Jurmark, B. S.; So, A. G.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 70, No. 12, 01.12.1973.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Reticulocyte RNA dependent RNA polymerase
AU - Downey, K. M.
AU - Byrnes, John
AU - Jurmark, B. S.
AU - So, A. G.
PY - 1973/12/1
Y1 - 1973/12/1
N2 - 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.
AB - 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.
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M3 - Article
C2 - 4519633
AN - SCOPUS:0015760851
VL - 70
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 12
ER -