| pubmed-article:11050188 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11050188 | lifeskim:mentions | umls-concept:C0162571 | lld:lifeskim |
| pubmed-article:11050188 | lifeskim:mentions | umls-concept:C0042153 | lld:lifeskim |
| pubmed-article:11050188 | lifeskim:mentions | umls-concept:C0012892 | lld:lifeskim |
| pubmed-article:11050188 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:11050188 | lifeskim:mentions | umls-concept:C0206415 | lld:lifeskim |
| pubmed-article:11050188 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:11050188 | pubmed:dateCreated | 2000-11-27 | lld:pubmed |
| pubmed-article:11050188 | pubmed:abstractText | The three-dimensional structure of bacteriophage T7 DNA polymerase reveals the presence of a loop of 4 aa (residues 401-404) within the DNA-binding groove; this loop is not present in other members of the DNA polymerase I family. A genetically altered T7 DNA polymerase, T7 polDelta401-404, lacking these residues, has been characterized biochemically. The polymerase activity of T7 polDelta401-404 on primed M13 single-stranded DNA template is one-third of the wild-type enzyme and has a 3'-to-5' exonuclease activity indistinguishable from that of wild-type T7 DNA polymerase. T7 polDelta401-404 polymerizes nucleotides processively on a primed M13 single-stranded DNA template. T7 DNA polymerase cannot initiate de novo DNA synthesis; it requires tetraribonucleotides synthesized by the primase activity of the T7 gene 4 protein to serve as primers. T7 primase-dependent DNA synthesis on single-stranded DNA is 3- to 6-fold less with T7 polDelta401-404 compared with the wild-type enzyme. Furthermore, the altered polymerase is defective (10-fold) in its ability to use preformed tetraribonucleotides to initiate DNA synthesis in the presence of gene 4 protein. The location of the loop places it in precisely the position to interact with the tetraribonucleotide primer and, presumably, with the T7 gene 4 primase. Gene 4 protein also provides helicase activity for the replication of duplex DNA. T7 polDelta401-404 and T7 gene 4 protein catalyze strand-displacement DNA synthesis at nearly the same rate as does wild-type polymerase and T7 gene 4 protein, suggesting that the coupling of helicase and polymerase activities is unaffected. | lld:pubmed |
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| pubmed-article:11050188 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11050188 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11050188 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11050188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11050188 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11050188 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11050188 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11050188 | pubmed:author | pubmed-author:ChowdhuryKK | lld:pubmed |
| pubmed-article:11050188 | pubmed:author | pubmed-author:RichardsonC... | lld:pubmed |
| pubmed-article:11050188 | pubmed:author | pubmed-author:TaborSS | lld:pubmed |
| pubmed-article:11050188 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11050188 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:11050188 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:11050188 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11050188 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11050188 | pubmed:pagination | 12469-74 | lld:pubmed |
| pubmed-article:11050188 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:meshHeading | pubmed-meshheading:11050188... | lld:pubmed |
| pubmed-article:11050188 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11050188 | pubmed:articleTitle | A unique loop in the DNA-binding crevice of bacteriophage T7 DNA polymerase influences primer utilization. | lld:pubmed |
| pubmed-article:11050188 | pubmed:affiliation | Department of Biological Chemistry and Molecular Pharmacology, Harvard University Medical School, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:11050188 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11050188 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
