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http://purl.uniprot.org/citations/15542682http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15542682http://www.w3.org/2000/01/rdf-schema#comment"The RNase H cleavages that generate and remove the polypurine tract (PPT) primer during retroviral reverse transcription must be specific in order to create a linear viral DNA that is suitable for integration. Lentiviruses contain a highly conserved sequence consisting of six guanine residues at the 3' end of the PPT (hereafter referred to as the G tract). We introduced mutations into the G tract of a human immunodeficiency virus type 1-based vector and determined the effects on the virus titer and RNase H cleavage specificity. Most mutations in the G tract had little or no effect on the virus titer. Mutations at the second and fifth positions of the G tract increased the proportion of two-long-terminal-repeat (2-LTR) circle junctions with one or two nucleotide insertions. The second and fifth positions of the G tract make specific contacts with amino acids in the RNase H domain that are important for RNase H cleavage specificity. These complementary data define protein-nucleic acid interactions that help control the specificity of RNase H cleavage. When the G-tract mutants were analyzed in a viral background that was deficient in integrase, in most cases the proportion of consensus 2-LTR circle junctions increased. However, in the case of a mutant with Ts at the second and fifth positions of the G tract, the proportion of 2-LTR circle junctions containing the one-nucleotide insertion increased, suggesting that linear viral DNAs containing an extra base are substrates for integration. This result is consistent with the idea that the 3' end-processing reactions of retroviral integrases may help to generate defined ends from a heterogenous population of linear viral DNAs."xsd:string
http://purl.uniprot.org/citations/15542682http://purl.org/dc/terms/identifier"doi:10.1128/jvi.78.23.13315-13324.2004"xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/author"Arnold E."xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/author"Hughes S.H."xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/author"Sarafianos S.G."xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/author"McWilliams M.J."xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/author"Alvord W.G."xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/author"Julias J.G."xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/name"J Virol"xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/pages"13315-13324"xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/title"Effects of mutations in the G tract of the human immunodeficiency virus type 1 polypurine tract on virus replication and RNase H cleavage."xsd:string
http://purl.uniprot.org/citations/15542682http://purl.uniprot.org/core/volume"78"xsd:string
http://purl.uniprot.org/citations/15542682http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15542682
http://purl.uniprot.org/citations/15542682http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15542682
http://purl.uniprot.org/uniprot/#_P62937-mappedCitation-15542682http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15542682
http://purl.uniprot.org/uniprot/P62937http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15542682