pubmed-article:1112826 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1112826 | lifeskim:mentions | umls-concept:C0004651 | lld:lifeskim |
pubmed-article:1112826 | lifeskim:mentions | umls-concept:C0085470 | lld:lifeskim |
pubmed-article:1112826 | lifeskim:mentions | umls-concept:C0035681 | lld:lifeskim |
pubmed-article:1112826 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:1112826 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:1112826 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:1112826 | pubmed:dateCreated | 1975-5-21 | lld:pubmed |
pubmed-article:1112826 | pubmed:abstractText | Infection of Pseudomonas putida by the bacteriophage gh-L-induced the synthesis of a novel DNA-dependent RNA polymerase. This gh-L-induced RNA polymerase was purified to near homogeneity. It was shown to be distinct from the host RNA polymerase (alpha-2 beta beta sigma) physically and in respect to many of its catalytic properties. The gh-L-induced RNA polymerase was composed of a single polypeptide of approximately 98,000 molecular weight. The divalent metal ion requirement for in vitro RNA synthesis by the gh-L-polymerase could be satisified with Mg-2+, but not with Mn-2+. Rna synthesis by the gh-L polymerase was highly resistant to inhibition by rifampicin and streptolydigin but could be inhibited by relatively low concentrations of KCl or the rifamycin derivative AF/013. The structural analog of ATP, 3'-deoxyadenosine 5'-triphosphate, inhibited both the gh-L-induced and the host RNA polymerases by competing for a single binding site with ATP. The phage polymerase was extremely sensitive to this inhibitor, exhibiting an apparent K-i value (2 times 10-8 M) approximately 100 times lower than that for the host RNA polymerase. The gh-L polymerase had a highly specific template requirement for DNA from the homologous gh-L phage. It would not efficiently utilize denatured DNA templates and had only low levels of activity with pyrimidine-containing polydeoxyribonucleotide homopolymers. | lld:pubmed |
pubmed-article:1112826 | pubmed:language | eng | lld:pubmed |
pubmed-article:1112826 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1112826 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1112826 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1112826 | pubmed:month | Mar | lld:pubmed |
pubmed-article:1112826 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1112826 | pubmed:author | pubmed-author:BoeziJ AJA | lld:pubmed |
pubmed-article:1112826 | pubmed:author | pubmed-author:TowleH CHC | lld:pubmed |
pubmed-article:1112826 | pubmed:author | pubmed-author:JollyJ FJF | lld:pubmed |
pubmed-article:1112826 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1112826 | pubmed:day | 10 | lld:pubmed |
pubmed-article:1112826 | pubmed:volume | 250 | lld:pubmed |
pubmed-article:1112826 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1112826 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1112826 | pubmed:pagination | 1723-33 | lld:pubmed |
pubmed-article:1112826 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:1112826 | pubmed:year | 1975 | lld:pubmed |
pubmed-article:1112826 | pubmed:articleTitle | Purification and characterization of bacteriophage gh-I-induced deoxyribonucleic acid-dependent ribonucleic acid polymerase from Pseudomonas putida. | lld:pubmed |
pubmed-article:1112826 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1112826 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:1112826 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1112826 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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