Journal
NUCLEIC ACIDS RESEARCH
Volume 50, Issue 4, Pages 1815-1828Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkac052
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Funding
- European Research Council, Horizon 2020 Framework Programmes [322581]
- National Institutes of Health [GM34360]
- Adams Foundation
- Kimmelman Center for Macromolecular Assemblies
- Martin S. and Helen Kimmel Professorial Chair at the Weizmann Institute of Science
- Horizon 2020 Framework Programmes grant
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This study demonstrates that several protoribosome constructs have the ability to mediate peptide-bond formation, providing strong evidence for the hypothesis on the origin of life and the construction of ribosomes. These findings suggest that the protoribosome may serve as the missing link between the RNA dominated world and the contemporary nucleic acids/proteins life.
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.
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