Literature DB >> 22245970

Molecular basis for RNA polymerization by Qβ replicase.

Daijiro Takeshita1, Kozo Tomita.   

Abstract

Core Qβ replicase comprises the Qβ virus-encoded RNA-dependent RNA polymerase (β-subunit) and the host Escherichia coli translational elongation factors EF-Tu and EF-Ts. The functions of the host proteins in the viral replicase are not clear. Structural analyses of RNA polymerization by core Qβ replicase reveal that at the initiation stage, the 3'-adenine of the template RNA provides a stable platform for de novo initiation. EF-Tu in Qβ replicase forms a template exit channel with the β-subunit. At the elongation stages, the C-terminal region of the β-subunit, assisted by EF-Tu, splits the temporarily double-stranded RNA between the template and nascent RNAs before translocation of the single-stranded template RNA into the exit channel. Therefore, EF-Tu in Qβ replicase modulates RNA elongation processes in a distinct manner from its established function in protein synthesis.

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Year:  2012        PMID: 22245970     DOI: 10.1038/nsmb.2204

Source DB:  PubMed          Journal:  Nat Struct Mol Biol        ISSN: 1545-9985            Impact factor:   15.369


  50 in total

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Journal:  Nat Struct Biol       Date:  1997-08

7.  Chaperone properties of bacterial elongation factor EF-Tu.

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Journal:  J Biol Chem       Date:  1998-05-08       Impact factor: 5.157

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  20 in total

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10.  Evolution of tertiary structure of viral RNA dependent polymerases.

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Journal:  PLoS One       Date:  2014-05-09       Impact factor: 3.240

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