Transcription of RNA polymerase binding sites isolated from T4 phage DNA
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, ISSN: 0005-2787, Vol: 238, Issue: 2, Page: 202-211
1971
- 18Citations
- 1Captures
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Metrics Details
- Citations18
- Citation Indexes18
- CrossRef18
- 13
- Captures1
- Readers1
Article Description
RNA polymerase (nucleoside triphosphate: RNA nucleotidyltransferase, DNA-dependent, EC 2.7.7.6) was bound to T4 DNA. After extensive digestion with deoxyribonuclease, DNA regions protected by the polymerase against the nucleolytic action were isolated. The template activity of these DNA fragments in the RNA polymerase reaction was studied by varying the salt concentrations and by the addition of deoxyribonuclease, ribonuclease, rifampicin and streptolydigin 1.1. These DNA fragments serve as templates for RNA transcription. The reaction is not markedly influenced by the KCl concentration. Once the polymerase is bound to the isolated DNA fragments further addition of deoxyribonuclease does not reduce the incorporation of ribonucleotides. Rifampicin, streptolydigin or the lack of one of the four ribotriphosphates stops the reaction.2.2. The transcription product is composed of AMP, CMP, GMP and UMP. From hybridization experiments the chain length of the synthesized RNA was estimated to be 15–20 ribonucleotides. The transcription product hybridizes specifically with T4 DNA.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0005278771900876; http://dx.doi.org/10.1016/0005-2787(71)90087-6; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0015221939&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/4936433; https://linkinghub.elsevier.com/retrieve/pii/0005278771900876; http://dx.doi.org/10.1016/0005-2787%2871%2990087-6; https://dx.doi.org/10.1016/0005-2787%2871%2990087-6
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