| Literature DB >> 35137169 |
Tanaya Bose1, Gil Fridkin1,2, Chen Davidovich1, Miri Krupkin1, Nikita Dinger1, Alla H Falkovich1, Yoav Peleg3, Ilana Agmon4,5, Anat Bashan1, Ada Yonath1.
Abstract
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.Entities:
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Year: 2022 PMID: 35137169 PMCID: PMC8886871 DOI: 10.1093/nar/gkac052
Source DB: PubMed Journal: Nucleic Acids Res ISSN: 0305-1048 Impact factor: 16.971