pubmed-article:8663453 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8663453 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
pubmed-article:8663453 | lifeskim:mentions | umls-concept:C0012892 | lld:lifeskim |
pubmed-article:8663453 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:8663453 | pubmed:issue | 30 | lld:pubmed |
pubmed-article:8663453 | pubmed:dateCreated | 1996-9-3 | lld:pubmed |
pubmed-article:8663453 | pubmed:abstractText | We show that archaebacterial DNA polymerases are strongly inhibited by the presence of small amounts of uracil-containing DNA. Inhibition appears to be competitive, with the DNA polymerase exhibiting approximately 6500-fold greater affinity for binding the inhibitor than a DNase I-activated DNA substrate. All six archaebacterial DNA polymerases tested were inhibited, while no eubacterial, eukaryotic, or bacteriophage enzymes showed this effect. Only a small inhibition resulted when uracil was present as the deoxynucleoside triphosphate, dUTP. The rate of DNA synthesis was reduced by approximately 40% when dUTP was used in place of dTTP for archaebacterial DNA polymerases. Furthermore, an incorporated dUMP served as a productive 3'-primer terminus for subsequent elongation. In contrast, the presence of an oligonucleotide containing as little as a single dUrd residue was extremely inhibitory to DNA polymerase activity on other primer-template DNA. | lld:pubmed |
pubmed-article:8663453 | pubmed:language | eng | lld:pubmed |
pubmed-article:8663453 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8663453 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8663453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8663453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8663453 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8663453 | pubmed:month | Jul | lld:pubmed |
pubmed-article:8663453 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:8663453 | pubmed:author | pubmed-author:RashtchianAA | lld:pubmed |
pubmed-article:8663453 | pubmed:author | pubmed-author:SchusterD MDM | lld:pubmed |
pubmed-article:8663453 | pubmed:author | pubmed-author:LaskenR SRS | lld:pubmed |
pubmed-article:8663453 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8663453 | pubmed:day | 26 | lld:pubmed |
pubmed-article:8663453 | pubmed:volume | 271 | lld:pubmed |
pubmed-article:8663453 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8663453 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8663453 | pubmed:pagination | 17692-6 | lld:pubmed |
pubmed-article:8663453 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:8663453 | pubmed:meshHeading | pubmed-meshheading:8663453-... | lld:pubmed |
pubmed-article:8663453 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8663453 | pubmed:articleTitle | Archaebacterial DNA polymerases tightly bind uracil-containing DNA. | lld:pubmed |
pubmed-article:8663453 | pubmed:affiliation | Life Technologies, Inc., Gaithersburg, Maryland 20884-9980, USA. | lld:pubmed |
pubmed-article:8663453 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8663453 | pubmed:publicationType | Comparative Study | lld:pubmed |
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