ArticleThe Biochemical journal2002
Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Oxidative stress sensing by the translation elongation machinery promotes production of detoxifying selenoproteins.bioRxiv : the preprint server for biology · 2025Article
- Multidimensional Regulatory Mechanisms and Targeting Strategies of the eEF1 Family in RNA Virus Infection.Viruses · 2025Review
- EEF1B2 regulates bone marrow-derived mesenchymal stem cells bone-fat balance via Wnt/β-catenin signaling.Cellular and molecular life sciences : CMLS · 2024Article
- eEF1A2 promotes PTEN-GSK3β-SCF complex-dependent degradation of Aurora kinase A and is inactivated in breast cancer.Science signaling · 2024Article
- The eEF1 family of mammalian translation elongation factors.BBA advances · 2023Article
- Quaternary organization of the human eEF1B complex reveals unique multi-GEF domain assembly.Nucleic acids research · 2022Article
- The pseudogenes of eukaryotic translation elongation factors (EEFs): Role in cancer and other human diseases.Genes & diseases · 2022Review
- Eukaryotic Translation Elongation Factor 1 Delta Inhibits the Nuclear Import of the Nucleoprotein and PA-PB1 Heterodimer of Influenza A Virus.Journal of virology · 2020Article
- Article
- Strain-Specific Contribution of Eukaryotic Elongation Factor 1 Gamma to the Translation of Influenza A Virus Proteins.Frontiers in microbiology · 2018Article
- Translation Elongation Factor eEF1A2 is a Novel Anticancer Target for the Marine Natural Product Plitidepsin.Scientific reports · 2016Article
- The C-terminal region of human eukaryotic elongation factor 1Bδ.Journal of biomolecular NMR · 2016Article
- Aminoacyl-tRNA synthetase complexes in evolution.International journal of molecular sciences · 2015Review
- Article
- Eukaryotic elongation factor 1 complex subunits are critical HIV-1 reverse transcription cofactors.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Mitotic modulation of translation elongation factor 1 leads to hindered tRNA delivery to ribosomes.The Journal of biological chemistry · 2011Article
- Caenorhabditis elegans evolves a new architecture for the multi-aminoacyl-tRNA synthetase complex.The Journal of biological chemistry · 2011Article
- Article
- Article
- Translation elongation factor eEF1A binds to a novel myosin binding protein-C-like protein.Journal of cellular biochemistry · 2008Article
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes, the eukaryotic translation elongation factor eEF1A responsible for transporting amino-acylated tRNA to the ribosome forms a higher-order complex, eEF1H, with its guanine-nucleotide-exchange factor eEF1B. In metazoans, eEF1B consists of three subunits: eEF1B alpha, eEF1B eta and eEF1B gamma. The first two subunits possess the nucleotide-exchange activity, whereas the role of the last remains poorly defined. In mammals, two active tissue-specific isoforms of eEF1A have been identified. The reason for this pattern of differential expression is unknown. Several models on the basis of in vitro experiments have been proposed for the macromolecular organization of the eEF1H complex. However, these models differ in various aspects. This might be due to the difficulties of handling, particularly the eEF1B beta and eEF1B gamma subunits in vitro. Here, the human eEF1H complex is for the first time mapped using the yeast two-hybrid system, which is a powerful in vivo technique for analysing protein-protein interactions. The following complexes were observed: eEF1A1:eEF1B alpha, eEF1A1:eEF1B beta, eEF1B beta:eEF1B beta, eEF1B alpha:eEF1B gamma, eEF1B beta:eEF1B gamma and eEF1B alpha:eEF1B gamma:eEF1B beta, where the last was observed using a three-hybrid approach. Surprisingly, eEF1A2 showed no or only little affinity for the guanine-nucleotide-exchange factors. Truncated versions of the subunits of eEF1B were used to orientate these subunits within the resulting model. The model unit is a pentamer composed of two molecules of eEF1A, each interacting with either eEF1B alpha or eEF1B beta held together by eEF1B gamma. These units can dimerize via eEF1B beta. Our model is compared with other models, and structural as well as functional aspects of the model are discussed.
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