| http://purl.uniprot.org/citations/12206668 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12206668 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12206668 | http://www.w3.org/2000/01/rdf-schema#comment | "The RNase H activity of HIV-RT is coordinated by a catalytic triad (E478, D443, D498) of acidic residues that bind divalent cations. We examined the effect of RNase H deficient E(478)-->Q and D(549)-->N mutations that do not alter polymerase activity on binding of enzyme to various nucleic acid substrates. Binding of the mutant and wild-type enzymes to various nucleic acid substrates was examined by determining dissociation rate constants (k(off)) by titrating both Mg(2+) and salt concentrations. In agreement with the unaltered polymerase activity of the mutant, the k(off) values for the wild-type and mutant enzymes were essentially identical using DNA-DNA templates in the presence of 6 mM Mg(2+). However, with lower concentrations of Mg(2+) and in the absence of Mg(2+), although both enzymes dissociated more rapidly, the mutant enzymes dissociated several-fold more slowly than the wild type. This was also observed on RNA-DNA templates. These results indicate that alterations in residues essential for Mg(2+) binding have a pronounced positive effect on enzyme-template stability and that the negative residues in the RNase H region of the enzyme have a negative influence on binding in the absence of Mg(2+). In this regard RT is similar to other nucleic acid cleaving enzymes that show enhanced binding upon mutation of active site residues."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi025871v"xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi025871v"xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/author | "Cristofaro J.V."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/author | "Cristofaro J.V."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/author | "DeStefano J.J."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/author | "DeStefano J.J."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/author | "Le Grice S.F."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/author | "Le Grice S.F."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/author | "Rausch J.W."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/author | "Rausch J.W."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/pages | "10968-10975"xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/pages | "10968-10975"xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/title | "Mutations in the ribonuclease H active site of HIV-RT reveal a role for this site in stabilizing enzyme-primer-template binding."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/title | "Mutations in the ribonuclease H active site of HIV-RT reveal a role for this site in stabilizing enzyme-primer-template binding."xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/volume | "41"xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://purl.uniprot.org/core/volume | "41"xsd:string |
| http://purl.uniprot.org/citations/12206668 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12206668 |
| http://purl.uniprot.org/citations/12206668 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12206668 |