ArticlePloS one2011
Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferases.
Article in PloS one, 2011. 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, 26 citations in OpenAlex.
- Insights into the role of legionella effectors on host metabolic perturbations.Frontiers in cellular and infection microbiology · 2024Review
- Legionella pneumophila-mediated host posttranslational modifications.Journal of molecular cell biology · 2023Review
- A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle.Molecular cell · 2023Article
- The genome of a hadal sea cucumber reveals novel adaptive strategies to deep-sea environments.iScience · 2022Article
- Glycosylating Effectors ofBiomolecules · 2022Review
- Pathogenicity and Virulence ofVirulence · 2021Review
- Non-canonical activation of the ER stress sensor ATF6 byLife science alliance · 2021Article
- Remodeling of host glycoproteins during bacterial infection.BMB reports · 2021Review
- The Legionella pneumophila Metaeffector Lpg2505 (MesI) Regulates SidI-Mediated Translation Inhibition and Novel Glycosyl Hydrolase Activity.Infection and immunity · 2020Article
- Targeting Eukaryotic mRNA Translation byFrontiers in molecular biosciences · 2020Review
- Article
- Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.The Journal of biological chemistry · 2017Article
- Article
- Elongation factor 1A is the target of growth inhibition in yeast caused by Legionella pneumophila glucosyltransferase Lgt1.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Legionella pneumophila, which is the causative organism of Legionnaireś disease, translocates numerous effector proteins into the host cell cytosol by a type IV secretion system during infection. Among the most potent effector proteins of Legionella are glucosyltransferases (lgt's), which selectively modify eukaryotic elongation factor (eEF) 1A at Ser-53 in the GTP binding domain. Glucosylation results in inhibition of protein synthesis. Here we show that in vitro glucosylation of yeast and mouse eEF1A by Lgt3 in the presence of the factors Phe-tRNA(Phe) and GTP was enhanced 150 and 590-fold, respectively. The glucosylation of eEF1A catalyzed by Lgt1 and 2 was increased about 70-fold. By comparison of uncharged tRNA with two distinct aminoacyl-tRNAs (His-tRNA(His) and Phe-tRNA(Phe)) we could show that aminoacylation is crucial for Lgt-catalyzed glucosylation. Aminoacyl-tRNA had no effect on the enzymatic properties of lgt's and did not enhance the glucosylation rate of eEF1A truncation mutants, consisting of the GTPase domain only or of a 5 kDa peptide covering Ser-53 of eEF1A. Furthermore, binding of aminoacyl-tRNA to eEF1A was not altered by glucosylation. Taken together, our data suggest that the ternary complex, consisting of eEF1A, aminoacyl-tRNA and GTP, is the bona fide substrate for lgt's.
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