Life began with the emergence of a molecule that could replicate its own genetic material, a task plausibly mediated by an RNA-dependent RNA polymerase ribozyme. Here, we present the structure of such a polymerase ribozyme, bound to RNA substrates comprising the template, primer, and nucleoside triphosphate (NTP) analog. The structure reveals how directed evolution shaped flanking elements around a highly conserved catalytic core derived from the ancestral class I ligase ribozyme. Each element serves as a functional module, positioning the primer-template duplex and incoming NTP within the active site of the enzyme. This emergent domain organization is remarkably similar to the "right hand" configuration of polymerase proteins, suggesting a common functional form for copying nucleic acids, regardless of biopolymer catalyst.
Strutzenberg, T. S., Horning, D. P., Cochrane, W. G., Andrade, L., Han, X., Joyce, G. F., Lyumkis, D.
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