ArticleNucleic acids research2013
Roles of yeast eIF2α and eIF2β subunits in the binding of the initiator methionyl-tRNA.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Substrate Binding Relieves Autoinhibition of the Mammalian GCN2 Kinase.bioRxiv : the preprint server for biology · 2026Article
- eIF2B localization and its regulation during the integrated stress response is cell-type specific.iScience · 2024Article
- Small GTP-binding protein GDP dissociation stimulator influences cisplatin-induced acute kidney injury via PERK-dependent ER stress.Communications biology · 2024Article
- Role of aIF5B in archaeal translation initiation.Nucleic acids research · 2022Article
- Elucidation of the Translation Initiation Factor Interaction Network ofFrontiers in microbiology · 2021Article
- Start Codon Recognition in Eukaryotic and Archaeal Translation Initiation: A Common Structural Core.International journal of molecular sciences · 2019Review
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
- eIF2A, an initiator tRNA carrier refractory to eIF2α kinases, functions synergistically with eIF5B.Cellular and molecular life sciences : CMLS · 2018Article
- Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes.eLife · 2017Article
- Cryo-EM study of start codon selection during archaeal translation initiation.Nature communications · 2016Article
- Interaction of tRNA with eukaryotic ribosome.International journal of molecular sciences · 2015Review
- eIF2 interactions with initiator tRNA and eIF2B are regulated by post-translational modifications and conformational dynamics.Cell discovery · 2015Article
- eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core.Nature communications · 2014Article
- Structure of the mammalian ribosomal 43S preinitiation complex bound to the scanning factor DHX29.Cell · 2013Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Heterotrimeric eukaryotic/archaeal translation initiation factor 2 (e/aIF2) binds initiator methionyl-tRNA and plays a key role in the selection of the start codon on messenger RNA. tRNA binding was extensively studied in the archaeal system. The γ subunit is able to bind tRNA, but the α subunit is required to reach high affinity whereas the β subunit has only a minor role. In Saccharomyces cerevisiae however, the available data suggest an opposite scenario with β having the most important contribution to tRNA-binding affinity. In order to overcome difficulties with purification of the yeast eIF2γ subunit, we designed chimeric eIF2 by assembling yeast α and β subunits to archaeal γ subunit. We show that the β subunit of yeast has indeed an important role, with the eukaryote-specific N- and C-terminal domains being necessary to obtain full tRNA-binding affinity. The α subunit apparently has a modest contribution. However, the positive effect of α on tRNA binding can be progressively increased upon shortening the acidic C-terminal extension. These results, together with small angle X-ray scattering experiments, support the idea that in yeast eIF2, the tRNA molecule is bound by the α subunit in a manner similar to that observed in the archaeal aIF2-GDPNP-tRNA complex.
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