ArticleBiology direct2010
GTPases and the origin of the ribosome.
Article in Biology direct, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 26 citations in OpenAlex.
- Science of the gaps.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- Early divergence of translation initiation and elongation factors.Protein science : a publication of the Protein Society · 2022Article
- High-resolution structures of a thermophilic eukaryotic 80S ribosome reveal atomistic details of translocation.Nature communications · 2022Article
- History of the ribosome and the origin of translation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The evolution of the ribosome and the genetic code.Life (Basel, Switzerland) · 2014Article
- Integration of latex protein sequence data provides comprehensive functional overview of latex proteins.Molecular biology reports · 2014Article
- CPEB2-eEF2 interaction impedes HIF-1α RNA translation.The EMBO journal · 2012Article
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2 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThis paper is an attempt to trace the evolution of the ribosome through the evolution of the universal P-loop GTPases that are involved with the ribosome in translation and with the attachment of the ribosome to the membrane. The GTPases involved in translation in Bacteria/Archaea are the elongation factors EFTu/EF1, the initiation factors IF2/aeIF5b + aeIF2, and the elongation factors EFG/EF2. All of these GTPases also contain the OB fold also found in the non GTPase IF1 involved in initiation. The GTPase involved in the signal recognition particle in most Bacteria and Archaea is SRP54.
results1) The Elongation Factors of the Archaea based on structural considerations of the domains have the following evolutionary path: EF1--> aeIF2 --> EF2. The evolution of the aeIF5b was a later event; 2) the Elongation Factors of the Bacteria based on the topological considerations of the GTPase domain have a similar evolutionary path: EFTu--> IF-->2-->EFG. These evolutionary sequences reflect the evolution of the LSU followed by the SSU to form the ribosome; 3) the OB-fold IF1 is a mimic of an ancient tRNA minihelix.
conclusionThe evolution of translational GTPases of both the Archaea and Bacteria point to the evolution of the ribosome. The elongation factors, EFTu/EF1, began as a Ras-like GTPase bringing the activated minihelix tRNA to the Large Subunit Unit. The initiation factors and elongation factor would then have evolved from the EFTu/EF1 as the small subunit was added to the evolving ribosome. The SRP has an SRP54 GTPase and a specific RNA fold in its RNA component similar to the PTC. We consider the SRP to be a remnant of an ancient form of an LSU bound to a membrane.
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