| pubmed-article:9843431 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9843431 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:9843431 | lifeskim:mentions | umls-concept:C0035379 | lld:lifeskim |
| pubmed-article:9843431 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:9843431 | lifeskim:mentions | umls-concept:C0598312 | lld:lifeskim |
| pubmed-article:9843431 | lifeskim:mentions | umls-concept:C1427199 | lld:lifeskim |
| pubmed-article:9843431 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9843431 | lifeskim:mentions | umls-concept:C0680011 | lld:lifeskim |
| pubmed-article:9843431 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:9843431 | pubmed:issue | 47 | lld:pubmed |
| pubmed-article:9843431 | pubmed:dateCreated | 1998-12-31 | lld:pubmed |
| pubmed-article:9843431 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:abstractText | The role of alpha-helix E' of the RNase H domain of human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) in template-primer binding and fidelity of DNA synthesis was investigated by using a series of mutant enzymes with deletions of 4, 8, 12, 16, and 20 amino acids at the C-terminal end of the 66 kDa subunit. The dissociation equilibrium constants (Kd) of wild-type HIV-1 RT and 38/16mer and 47/25mer DNA/DNA template-primer complexes were 2.2 +/- 0.7 and 0.69 +/- 0.35 nM, respectively. Deletions involving partial or total removal of alpha-helix E' rendered enzymes with a 2-5-fold decrease in binding affinity. Misinsertion and mispair extension fidelity of DNA synthesis of the wild-type enzyme and truncated mutants were determined by using both DNA/DNA template-primers and a 47/25mer RNA/DNA complex. In all cases, incorporation assays were done in the same sequence context, which was taken from the viral gag gene. The removal of alpha-helix E' had little effect on fidelity as determined with the three template-primers. Misinsertion fidelity assays showed that the specificity of mismatch formation was A:C approximately A:G > A:A for the DNA template and A:C > A:G approximately A:A for the RNA template, in 47/25mers. The specificity of extending mispaired 3'-termini was similar with both 47/25mers: A:C > A:A approximately A:G. However, the efficiency of transversion mispair extension was higher with RNA templates. The results reported in this paper suggest that alpha-helix E' may stabilize the RT/template-primer interaction, but does not have a strong influence in the correct positioning of the template-primer at the polymerase active site. | lld:pubmed |
| pubmed-article:9843431 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9843431 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9843431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9843431 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9843431 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9843431 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:9843431 | pubmed:author | pubmed-author:Menéndez-Aria... | lld:pubmed |
| pubmed-article:9843431 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9843431 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:9843431 | pubmed:volume | 37 | lld:pubmed |
| pubmed-article:9843431 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9843431 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9843431 | pubmed:pagination | 16636-44 | lld:pubmed |
| pubmed-article:9843431 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:9843431 | pubmed:meshHeading | pubmed-meshheading:9843431-... | lld:pubmed |
| pubmed-article:9843431 | pubmed:meshHeading | pubmed-meshheading:9843431-... | lld:pubmed |
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| pubmed-article:9843431 | pubmed:meshHeading | pubmed-meshheading:9843431-... | lld:pubmed |
| pubmed-article:9843431 | pubmed:meshHeading | pubmed-meshheading:9843431-... | lld:pubmed |
| pubmed-article:9843431 | pubmed:meshHeading | pubmed-meshheading:9843431-... | lld:pubmed |
| pubmed-article:9843431 | pubmed:meshHeading | pubmed-meshheading:9843431-... | lld:pubmed |
| pubmed-article:9843431 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9843431 | pubmed:articleTitle | Studies on the effects of truncating alpha-helix E' of p66 human immunodeficiency virus type 1 reverse transcriptase on template-primer binding and fidelity of DNA synthesis. | lld:pubmed |
| pubmed-article:9843431 | pubmed:affiliation | Centro de Biología Molecular "Severo Ochoa", CSIC-Universidad Autónoma de Madrid, Spain. lmenedez@cbm.uam.es | lld:pubmed |
| pubmed-article:9843431 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9843431 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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