The Experts below are selected from a list of 39 Experts worldwide ranked by ideXlab platform
J. Michael Bishop - One of the best experts on this subject based on the ideXlab platform.
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The Classic: Integration of Deoxyribonucleic Acid Specific for Rous Sarcoma Virus after Infection of Permissive and Nonpermissive Hosts
Clinical Orthopaedics and Related Research, 2008Co-Authors: Harold E. Varmus, Peter K. Vogt, J. Michael BishopAbstract:A relatively simple but stringent technique was developed to detect the integration of Virus-specific DNA into the genomes of higher organisms. In both permissive (duck) and nonpermissive (mammalian) cells which normally contain no nucleotide sequences specific for Rous Sarcoma Virus, transformation by the Virus results in the appearance of DNA specific for Rous Sarcoma Virus covalently integrated into strands of host-cell DNA containing reiterated sequences. Early after infection of mouse or duck cells by Rous Sarcoma Virus, unintegrated DNA specific for the Virus can be demonstrated.
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Erratum: The Classic: Integration of Deoxyribonucleic Acid Specific for Rous Sarcoma Virus after Infection of Permissive and Nonpermissive Hosts
Clinical Orthopaedics and Related Research, 2008Co-Authors: Harold Varmus, Peter K. Vogt, J. Michael BishopAbstract:A relatively simple but stringent technique was developed to detect the integration of Virus-specific DNA into the genomes of higher organisms. In both permissive (duck) and nonpermissive (mammalian) cells which normally contain no nucleotide sequences specific for Rous Sarcoma Virus, transformation by the Virus results in the appearance of DNA specific for Rous Sarcoma Virus covalently integrated into strands of host-cell DNA containing reiterated sequences. Early after infection of mouse or duck cells by Rous Sarcoma Virus, unintegrated DNA specific for the Virus can be demonstrated.
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A comparison of the high molecular weight RNAs of visna Virus and Rous Sarcoma Virus.
Virology, 2004Co-Authors: Ashley T. Haase, Andanthony J. Faras, Axel C. Garapin, John M. Taylor, J. Michael BishopAbstract:Abstract Visna Virus RNA consists of a high molecular weight and low molecular weight species. The size, subunit composition, complexity, and secondary structure of high molecular weight RNA have been studied and compared with Rous Sarcoma Virus RNA. Visna high molecular weight RNA cosediments in 0.1 M sodium chloride wiih the 70S UNA of Rous Sarcoma Virus consistent with a molecular weight of 10–12 × 10 daltons. On dissociation with heat, subunit structures of 2.8 × 10 6 daltons are released. Both the size and heterogeneity of the subunit RNA are identical with the subunit RNA of transforming Schmidt-Ruppin Rous Sarcoma Virus. Comparison of the complexity of visna RNA with polioVirus RNA indicate unique nucleotide sequences of 7–10 × 10 6 daltons, in accord with the physical data. The evidence also indicates that there is lack of significant reiteration of nucleotide sequences in the visna RNA. Major differences in the secondary structure of visna and Rous Sarcoma Virus RNA were observed. Both RNAs possess an exceptional degree of secondary structure when assayed by chromatography on cellulose at various temperatures. Reduction of ionic srength markedly decreases the secondary structure of visna RNA relative to Rous Sarcoma Virus RNA and leads to anomalous migration in polyacrylamide gels. The differences in secondary structure and in the low molecular weight RNA species associated with 70S RNAs of these Viruses indirectly implicate the 4 and 5S RNA in the maintenance of secondary structure of 70S RNA of Rous Sarcoma Virus.
Peter K. Vogt - One of the best experts on this subject based on the ideXlab platform.
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100 years of Rous Sarcoma Virus
Journal of Experimental Medicine, 2011Co-Authors: Robin A Weiss, Peter K. VogtAbstract:The discovery of Rous Sarcoma Virus, which was reported by Peyton Rous in the Journal of Experimental Medicine 100 years ago, opened the field of tumor virology. It showed that some cancers have infectious etiology, led to the discovery of oncogenes, and laid the foundation for the molecular mechanisms of carcinogenesis. Rous spent his entire research career at The Rockefeller Institute, and he was the JEM ’s longest serving editor. Here, we comment briefly on the life of this remarkable scientist and on the importance of his discoveries.
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The Classic: Integration of Deoxyribonucleic Acid Specific for Rous Sarcoma Virus after Infection of Permissive and Nonpermissive Hosts
Clinical Orthopaedics and Related Research, 2008Co-Authors: Harold E. Varmus, Peter K. Vogt, J. Michael BishopAbstract:A relatively simple but stringent technique was developed to detect the integration of Virus-specific DNA into the genomes of higher organisms. In both permissive (duck) and nonpermissive (mammalian) cells which normally contain no nucleotide sequences specific for Rous Sarcoma Virus, transformation by the Virus results in the appearance of DNA specific for Rous Sarcoma Virus covalently integrated into strands of host-cell DNA containing reiterated sequences. Early after infection of mouse or duck cells by Rous Sarcoma Virus, unintegrated DNA specific for the Virus can be demonstrated.
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Erratum: The Classic: Integration of Deoxyribonucleic Acid Specific for Rous Sarcoma Virus after Infection of Permissive and Nonpermissive Hosts
Clinical Orthopaedics and Related Research, 2008Co-Authors: Harold Varmus, Peter K. Vogt, J. Michael BishopAbstract:A relatively simple but stringent technique was developed to detect the integration of Virus-specific DNA into the genomes of higher organisms. In both permissive (duck) and nonpermissive (mammalian) cells which normally contain no nucleotide sequences specific for Rous Sarcoma Virus, transformation by the Virus results in the appearance of DNA specific for Rous Sarcoma Virus covalently integrated into strands of host-cell DNA containing reiterated sequences. Early after infection of mouse or duck cells by Rous Sarcoma Virus, unintegrated DNA specific for the Virus can be demonstrated.
Hideki Aihara - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of the Rous Sarcoma Virus intasome
Nature, 2016Co-Authors: Surajit Banerjee, Krishan K Pandey, Sibes Bera, Duane P Grandgenett, Hideki AiharaAbstract:A crystal structure of the octameric integrase from Rous Sarcoma Virus in complex with viral and target DNAs. Integration of reverse-transcribed viral DNA into the host genome is an essential step in the life cycle of retroViruses, catalysed by the protein integrase. Two studies, from the laboratories of Hideki Aihara and Alan Engelman, have used crystallography and cryo-electron microscopy to determine the structure of Rous Sarcoma Virus and mouse mammary tumour Virus intasomes, the complex containing integrase, viral DNA, and target DNA. They find that integrase is an octameric assembly — not a tetramer as previously reported. A pair of core integrase dimers engages the viral DNA ends for catalysis, while another pair of non-catalytic integrase dimers bridge the two viral DNA molecules and help capture target DNA. The flanking, unanticipated pair of integrase dimers are required for target capture and strand transfer. Integration of the reverse-transcribed viral DNA into the host genome is an essential step in the life cycle of retroViruses. RetroVirus integrase catalyses insertions of both ends of the linear viral DNA into a host chromosome1. Integrase from HIV-1 and closely related retroViruses share the three-domain organization, consisting of a catalytic core domain flanked by amino- and carboxy-terminal domains essential for the concerted integration reaction. Although structures of the tetrameric integrase–DNA complexes have been reported for integrase from prototype foamy Virus featuring an additional DNA-binding domain and longer interdomain linkers2,3,4,5, the architecture of a canonical three-domain integrase bound to DNA remained elusive. Here we report a crystal structure of the three-domain integrase from Rous Sarcoma Virus in complex with viral and target DNAs. The structure shows an octameric assembly of integrase, in which a pair of integrase dimers engage viral DNA ends for catalysis while another pair of non-catalytic integrase dimers bridge between the two viral DNA molecules and help capture target DNA. The individual domains of the eight integrase molecules play varying roles to hold the complex together, making an extensive network of protein–DNA and protein–protein contacts that show both conserved and distinct features compared with those observed for prototype foamy Virus integrase. Our work highlights the diversity of retroVirus intasome assembly and provides insights into the mechanisms of integration by HIV-1 and related retroViruses.
Michael F Summers - One of the best experts on this subject based on the ideXlab platform.
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solution structure and dynamics of the Rous Sarcoma Virus capsid protein and comparison with capsid proteins of other retroViruses
Journal of Molecular Biology, 2000Co-Authors: Ramon Camposolivas, John L Newman, Michael F SummersAbstract:Abstract The solution structure and dynamics of the recombinant 240 amino acid residue capsid protein from the Rous Sarcoma Virus has been determined by NMR methods. The structure was determined using 2200 distance restraints and 330 torsion angle restraints, and the dynamics analysis was based on 15N relaxation parameters (R1, R2, and 1H-15N NOE) measured for 153 backbone amide groups. The monomeric protein consists of independently folded N- and C-terminal domains that comprise residues Leu14-Leu146 and Ala150-Gln226, respectively. The domains exhibit different rotational correlation times (16.6(±0.1) ns and 12.6(±0.1) ns, respectively), are connected by a flexible linker (Ala147-Pro149), and do not give rise to inter-domain NOE values, indicating that they are dynamically independent. Despite limited sequence similarity, the structure of the Rous Sarcoma Virus capsid protein is similar to the structures determined recently for the capsid proteins of retroViruses belonging to the lentiVirus and human T-cell leukemia Virus/bovine leukemia Virus genera. Structural differences that exist in the C-terminal domain of Rous Sarcoma Virus capsid relative to the other capsid proteins appear to be related to the occurrence of conserved cysteine residues. Whereas most genera of retroViruses contain a pair of conserved and essential cysteine residues in the C-terminal domain that appear to function by forming an intramolecular disulfide bond during assembly, the Rous Sarcoma Virus capsid protein does not. Instead, the Rous Sarcoma Virus capsid protein contains a single cysteine residue that appears to be conserved among the avian C-type retroViruses and is positioned in a manner that might allow the formation of an intermolecular disulfide bond during capsid assembly.
Surajit Banerjee - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of the Rous Sarcoma Virus intasome
Nature, 2016Co-Authors: Surajit Banerjee, Krishan K Pandey, Sibes Bera, Duane P Grandgenett, Hideki AiharaAbstract:A crystal structure of the octameric integrase from Rous Sarcoma Virus in complex with viral and target DNAs. Integration of reverse-transcribed viral DNA into the host genome is an essential step in the life cycle of retroViruses, catalysed by the protein integrase. Two studies, from the laboratories of Hideki Aihara and Alan Engelman, have used crystallography and cryo-electron microscopy to determine the structure of Rous Sarcoma Virus and mouse mammary tumour Virus intasomes, the complex containing integrase, viral DNA, and target DNA. They find that integrase is an octameric assembly — not a tetramer as previously reported. A pair of core integrase dimers engages the viral DNA ends for catalysis, while another pair of non-catalytic integrase dimers bridge the two viral DNA molecules and help capture target DNA. The flanking, unanticipated pair of integrase dimers are required for target capture and strand transfer. Integration of the reverse-transcribed viral DNA into the host genome is an essential step in the life cycle of retroViruses. RetroVirus integrase catalyses insertions of both ends of the linear viral DNA into a host chromosome1. Integrase from HIV-1 and closely related retroViruses share the three-domain organization, consisting of a catalytic core domain flanked by amino- and carboxy-terminal domains essential for the concerted integration reaction. Although structures of the tetrameric integrase–DNA complexes have been reported for integrase from prototype foamy Virus featuring an additional DNA-binding domain and longer interdomain linkers2,3,4,5, the architecture of a canonical three-domain integrase bound to DNA remained elusive. Here we report a crystal structure of the three-domain integrase from Rous Sarcoma Virus in complex with viral and target DNAs. The structure shows an octameric assembly of integrase, in which a pair of integrase dimers engage viral DNA ends for catalysis while another pair of non-catalytic integrase dimers bridge between the two viral DNA molecules and help capture target DNA. The individual domains of the eight integrase molecules play varying roles to hold the complex together, making an extensive network of protein–DNA and protein–protein contacts that show both conserved and distinct features compared with those observed for prototype foamy Virus integrase. Our work highlights the diversity of retroVirus intasome assembly and provides insights into the mechanisms of integration by HIV-1 and related retroViruses.
