| pubmed-article:10788512 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10788512 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:10788512 | lifeskim:mentions | umls-concept:C0028606 | lld:lifeskim |
| pubmed-article:10788512 | lifeskim:mentions | umls-concept:C0035379 | lld:lifeskim |
| pubmed-article:10788512 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10788512 | lifeskim:mentions | umls-concept:C1420280 | lld:lifeskim |
| pubmed-article:10788512 | lifeskim:mentions | umls-concept:C1419030 | lld:lifeskim |
| pubmed-article:10788512 | lifeskim:mentions | umls-concept:C0600401 | lld:lifeskim |
| pubmed-article:10788512 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:10788512 | pubmed:dateCreated | 2000-6-1 | lld:pubmed |
| pubmed-article:10788512 | pubmed:abstractText | The 55-kDa reverse transcriptase (RT) domain of the Ty3 POL3 open reading frame was purified and evaluated on conformationally distinct nucleic acid duplexes. Purified enzyme migrated as a monomer by size exclusion chromatography. Enzymatic footprinting indicate Ty3 RT protects template nucleotides +7 through -21 and primer nucleotides -1 through -24. Contrary to previous data with retroviral enzymes, a 4-base pair region of the template-primer duplex remained nuclease accessible. The C-terminal portion of Ty3 RT encodes a functional RNase H domain, although the hydrolysis profile suggests an increased spatial separation between the catalytic centers. Despite conservation of catalytically important residues in the RNase H domain, Fe(2+) fails to replace Mg(2+) in the RNase H catalytic center for localized generation of hydroxyl radicals, again suggesting this domain may be structurally distinct from its retroviral counterparts. RNase H specificity was investigated using a model system challenging the enzyme to select the polypurine tract primer from within an RNA/DNA hybrid, extend this into (+) DNA, and excise the primer from nascent DNA. Purified RT catalyzed each of these three steps but was almost inactive on a non-polypurine tract RNA primer. Our studies provide the first detailed characterization of the enzymatic activities of a retrotransposon reverse transcriptase. | lld:pubmed |
| pubmed-article:10788512 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788512 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788512 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10788512 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788512 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10788512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788512 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10788512 | pubmed:month | May | lld:pubmed |
| pubmed-article:10788512 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10788512 | pubmed:author | pubmed-author:MillerJ TJT | lld:pubmed |
| pubmed-article:10788512 | pubmed:author | pubmed-author:Le GriceS FSF | lld:pubmed |
| pubmed-article:10788512 | pubmed:author | pubmed-author:RauschJ WJW | lld:pubmed |
| pubmed-article:10788512 | pubmed:author | pubmed-author:HenriettaMM | lld:pubmed |
| pubmed-article:10788512 | pubmed:author | pubmed-author:GriceM KMK | lld:pubmed |
| pubmed-article:10788512 | pubmed:author | pubmed-author:Nymark-McMaho... | lld:pubmed |
| pubmed-article:10788512 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10788512 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:10788512 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10788512 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10788512 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10788512 | pubmed:pagination | 13879-87 | lld:pubmed |
| pubmed-article:10788512 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:meshHeading | pubmed-meshheading:10788512... | lld:pubmed |
| pubmed-article:10788512 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10788512 | pubmed:articleTitle | Interaction of p55 reverse transcriptase from the Saccharomyces cerevisiae retrotransposon Ty3 with conformationally distinct nucleic acid duplexes. | lld:pubmed |
| pubmed-article:10788512 | pubmed:affiliation | Human Immunodeficiency Virus Drug Resistance Program, Division of Basic Sciences, NCI-Frederick Cancer Research and Development Center, Frederick, Maryland 21702, USA. | lld:pubmed |
| pubmed-article:10788512 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10788512 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10788512 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10788512 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10788512 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10788512 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10788512 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10788512 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10788512 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10788512 | lld:pubmed |
