author_facet Kidmose, Rune T.
Vasiliev, Nikita N.
Chetverin, Alexander B.
Andersen, Gregers Rom
Knudsen, Charlotte R.
Kidmose, Rune T.
Vasiliev, Nikita N.
Chetverin, Alexander B.
Andersen, Gregers Rom
Knudsen, Charlotte R.
author Kidmose, Rune T.
Vasiliev, Nikita N.
Chetverin, Alexander B.
Andersen, Gregers Rom
Knudsen, Charlotte R.
spellingShingle Kidmose, Rune T.
Vasiliev, Nikita N.
Chetverin, Alexander B.
Andersen, Gregers Rom
Knudsen, Charlotte R.
Proceedings of the National Academy of Sciences
Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
Multidisciplinary
author_sort kidmose, rune t.
spelling Kidmose, Rune T. Vasiliev, Nikita N. Chetverin, Alexander B. Andersen, Gregers Rom Knudsen, Charlotte R. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1003015107 <jats:p> The RNA-dependent RNA polymerase core complex formed upon infection of <jats:italic>Escherichia coli</jats:italic> by the bacteriophage Qβ is composed of the viral catalytic β-subunit as well as the host translation elongation factors EF-Tu and EF-Ts, which are required for initiation of RNA replication. We have determined the crystal structure of the complex between the β-subunit and the two host proteins to 2.5-Å resolution. Whereas the basic catalytic machinery in the viral subunit appears similar to other RNA-dependent RNA polymerases, a unique C-terminal region of the β-subunit engages in extensive interactions with EF-Tu and may contribute to the separation of the transient duplex formed between the template and the nascent product to allow exponential amplification of the phage genome. The evolution of resistance by the host appears to be impaired because of the interactions of the β-subunit with parts of EF-Tu essential in recognition of aminoacyl-tRNA. </jats:p> Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins Proceedings of the National Academy of Sciences
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title Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_unstemmed Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_full Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_fullStr Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_full_unstemmed Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_short Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_sort structure of the qβ replicase, an rna-dependent rna polymerase consisting of viral and host proteins
topic Multidisciplinary
url http://dx.doi.org/10.1073/pnas.1003015107
publishDate 2010
physical 10884-10889
description <jats:p> The RNA-dependent RNA polymerase core complex formed upon infection of <jats:italic>Escherichia coli</jats:italic> by the bacteriophage Qβ is composed of the viral catalytic β-subunit as well as the host translation elongation factors EF-Tu and EF-Ts, which are required for initiation of RNA replication. We have determined the crystal structure of the complex between the β-subunit and the two host proteins to 2.5-Å resolution. Whereas the basic catalytic machinery in the viral subunit appears similar to other RNA-dependent RNA polymerases, a unique C-terminal region of the β-subunit engages in extensive interactions with EF-Tu and may contribute to the separation of the transient duplex formed between the template and the nascent product to allow exponential amplification of the phage genome. The evolution of resistance by the host appears to be impaired because of the interactions of the β-subunit with parts of EF-Tu essential in recognition of aminoacyl-tRNA. </jats:p>
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author Kidmose, Rune T., Vasiliev, Nikita N., Chetverin, Alexander B., Andersen, Gregers Rom, Knudsen, Charlotte R.
author_facet Kidmose, Rune T., Vasiliev, Nikita N., Chetverin, Alexander B., Andersen, Gregers Rom, Knudsen, Charlotte R., Kidmose, Rune T., Vasiliev, Nikita N., Chetverin, Alexander B., Andersen, Gregers Rom, Knudsen, Charlotte R.
author_sort kidmose, rune t.
container_issue 24
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container_title Proceedings of the National Academy of Sciences
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description <jats:p> The RNA-dependent RNA polymerase core complex formed upon infection of <jats:italic>Escherichia coli</jats:italic> by the bacteriophage Qβ is composed of the viral catalytic β-subunit as well as the host translation elongation factors EF-Tu and EF-Ts, which are required for initiation of RNA replication. We have determined the crystal structure of the complex between the β-subunit and the two host proteins to 2.5-Å resolution. Whereas the basic catalytic machinery in the viral subunit appears similar to other RNA-dependent RNA polymerases, a unique C-terminal region of the β-subunit engages in extensive interactions with EF-Tu and may contribute to the separation of the transient duplex formed between the template and the nascent product to allow exponential amplification of the phage genome. The evolution of resistance by the host appears to be impaired because of the interactions of the β-subunit with parts of EF-Tu essential in recognition of aminoacyl-tRNA. </jats:p>
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imprint Proceedings of the National Academy of Sciences, 2010
imprint_str_mv Proceedings of the National Academy of Sciences, 2010
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spelling Kidmose, Rune T. Vasiliev, Nikita N. Chetverin, Alexander B. Andersen, Gregers Rom Knudsen, Charlotte R. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1003015107 <jats:p> The RNA-dependent RNA polymerase core complex formed upon infection of <jats:italic>Escherichia coli</jats:italic> by the bacteriophage Qβ is composed of the viral catalytic β-subunit as well as the host translation elongation factors EF-Tu and EF-Ts, which are required for initiation of RNA replication. We have determined the crystal structure of the complex between the β-subunit and the two host proteins to 2.5-Å resolution. Whereas the basic catalytic machinery in the viral subunit appears similar to other RNA-dependent RNA polymerases, a unique C-terminal region of the β-subunit engages in extensive interactions with EF-Tu and may contribute to the separation of the transient duplex formed between the template and the nascent product to allow exponential amplification of the phage genome. The evolution of resistance by the host appears to be impaired because of the interactions of the β-subunit with parts of EF-Tu essential in recognition of aminoacyl-tRNA. </jats:p> Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins Proceedings of the National Academy of Sciences
spellingShingle Kidmose, Rune T., Vasiliev, Nikita N., Chetverin, Alexander B., Andersen, Gregers Rom, Knudsen, Charlotte R., Proceedings of the National Academy of Sciences, Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins, Multidisciplinary
title Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_full Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_fullStr Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_full_unstemmed Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_short Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
title_sort structure of the qβ replicase, an rna-dependent rna polymerase consisting of viral and host proteins
title_unstemmed Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
topic Multidisciplinary
url http://dx.doi.org/10.1073/pnas.1003015107