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Origin of life: protoribosome forms peptide bonds and links RNA and protein dominated worlds.

Tanaya BoseGil FridkinChen DavidovichMiri KrupkinNikita DingerAlla H FalkovichYoav PelegIlana AgmonAnat BashanAda Yonath
Published in: Nucleic acids research (2022)
Although the mode of action of the ribosomes, the multi-component universal effective protein-synthesis organelles, has been thoroughly explored, their mere appearance remained elusive. Our earlier comparative structural studies suggested that a universal internal small RNA pocket-like segment called by us the protoribosome, which is still embedded in the contemporary ribosome, is a vestige of the primordial ribosome. Herein, after constructing such pockets, we show using the "fragment reaction" and its analyses by MALDI-TOF and LC-MS mass spectrometry techniques, that several protoribosome constructs are indeed capable of mediating peptide-bond formation. These findings present strong evidence supporting our hypothesis on origin of life and on ribosome's construction, thus suggesting that the protoribosome may be the missing link between the RNA dominated world and the contemporary nucleic acids/proteins life.
Keyphrases
  • mass spectrometry
  • liquid chromatography
  • nucleic acid
  • high performance liquid chromatography
  • gas chromatography
  • capillary electrophoresis
  • small molecule
  • protein protein