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PreprintCC BYbioRxiv

Structure of an RNA polymerase ribozyme replication complex

  • T. S. Strutzenberg
  • D. P. Horning
  • W. G. Cochrane
  • L. Andrade
  • X. Han
  • G. F. Joyce
  • D. Lyumkis1
  1. 1The Salk Institute
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Abstract

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.

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Cite

BibTeXRIS
BibTeX
@misc{strutzenberg2026structure,
  title = {{Structure of an RNA polymerase ribozyme replication complex}},
  author = {T. S. Strutzenberg and D. P. Horning and W. G. Cochrane and L. Andrade and X. Han and G. F. Joyce and D. Lyumkis},
  howpublished = {bioRxiv},
  year = {2026},
  month = aug,
  doi = {10.64898/2026.08.30.748161},
  url = {https://www.biorxiv.org/content/10.64898/2026.08.30.748161v1},
  note = {CC BY},
}
RIS
TY  - UNPB
TI  - Structure of an RNA polymerase ribozyme replication complex
AU  - T. S. Strutzenberg
AU  - D. P. Horning
AU  - W. G. Cochrane
AU  - L. Andrade
AU  - X. Han
AU  - G. F. Joyce
AU  - D. Lyumkis
PY  - 2026
DA  - 2026/08/30
PB  - bioRxiv
DO  - 10.64898/2026.08.30.748161
UR  - https://www.biorxiv.org/content/10.64898/2026.08.30.748161v1
AB  - 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.
ER  -