ArticleMolecular microbiology2007
Functional analysis of the translation factor aIF2/5B in the thermophilic archaeon Sulfolobus solfataricus.
Article in Molecular microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 25 citations in OpenAlex.
- A widespread group of large plasmids in methanotrophic Methanoperedens archaea.Nature communications · 2022Article
- Role of aIF5B in archaeal translation initiation.Nucleic acids research · 2022Article
- Recent Advances in Archaeal Translation Initiation.Frontiers in microbiology · 2020Review
- eIF2A, an initiator tRNA carrier refractory to eIF2α kinases, functions synergistically with eIF5B.Cellular and molecular life sciences : CMLS · 2018Article
- Evolution of the archaeal and mammalian information processing systems: towards an archaeal model for human disease.Cellular and molecular life sciences : CMLS · 2017Review
- Four translation initiation pathways employed by the leaderless mRNA in eukaryotes.Scientific reports · 2016Article
- Article
- Why is start codon selection so precise in eukaryotes?Translation (Austin, Tex.) · 2014Review
- Omnipotent role of archaeal elongation factor 1 alpha (EF1α in translational elongation and termination, and quality control of protein synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Translation initiation complex formation in the crenarchaeon Sulfolobus solfataricus.RNA (New York, N.Y.) · 2009Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein IF2/eIF5B is one of the few translation initiation factors shared by all three primary domains of life (bacteria, archaea, eukarya). Despite its phylogenetic conservation, the factor is known to present marked functional divergences in the bacteria and the eukarya. In this work, the function in translation of the archaeal homologue (aIF2/5B) has been analysed in detail for the first time using a variety of in vitro assays. The results revealed that the protein is a ribosome-dependent GTPase which strongly stimulates the binding of initiator tRNA to the ribosomes even in the absence of other factors. In agreement with this finding, aIF2/5B enhances the translation of both leadered and leaderless mRNAs when expressed in a cell-free protein-synthesizing system. Moreover, the degree of functional conservation of the IF2-like factors in the archaeal and bacterial lineages was investigated by analysing the behaviour of 'chimeric' proteins produced by swapping domains between the Sulfolobus solfataricus aIF2/5B factor and the IF2 protein of the thermophilic bacterium Bacillus stearothermophilus. Beside evidencing similarities and differences between the archaeal and bacterial factors, these experiments have provided insight into the common role played by the IF2/5B proteins in all extant cells.
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