PMID:22245970

Citation	Takeshita, D and Tomita, K (2012) Molecular basis for RNA polymerization by Qβ replicase. Nat. Struct. Mol. Biol. 19:229-37
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.
Links	PubMed Online version:10.1038/nsmb.2204
Keywords	Escherichia coli/enzymology; Escherichia coli/virology; Peptide Elongation Factor Tu/metabolism; Peptide Elongation Factors/metabolism; Polymerization; Protein Multimerization; Q beta Replicase/metabolism; RNA, Viral/metabolism
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