Abstract
WITH the purification and characterization of viral replicases, a novel feature of nucleic acid polymerases—stringent template specificity—was recognized1,2. Qβ replicase, the most extensively studied viral RNA polymerase2–8, is now known to replicate Qβ RNA2, the complementary Qβ minus strand9, RNA molecules described as “variants” of Qβ RNA10,11, and a set of small RNAs of unknown origin which accumulate in Qβ-infected Escherichia coli, collectively designated as “6S RNA”12. On the other hand, the RNA from phages related distantly, if at all, to Qβ13,14, such as MS2 or R17, and of other viruses such as TMV2 or AMV (Diggelmann and Weissmann, unpublished results) are completely inert as templates, as are ribosomal and tRNA from E. coli2. Poly C and C-rich synthetic copolymers at high concentrations elicit synthesis which, however, remains restricted to the formation of a strand complementary to the template15,16.
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WEBER, H., BILLETER, M., KAHANE, S. et al. Molecular Basis for Repressor Activity of Qβ Replicase. Nature New Biology 237, 166–170 (1972). https://doi.org/10.1038/newbio237166a0
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DOI: https://doi.org/10.1038/newbio237166a0
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