ArticleThe Journal of biological chemistry2012
Elongation factor 1A is the target of growth inhibition in yeast caused by Legionella pneumophila glucosyltransferase Lgt1.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- The Legionella pneumophila effector SidL is an adenylyltransferase that modifies the glycolytic intermediate 3-phosphoglycerate.Molecular cell · 2026Article
- A comprehensive two-hybrid analysis to explore themSystems · 2024Article
- Unravelling bacterial virulence factors in yeast: From identification to the elucidation of their mechanisms of action.Archives of microbiology · 2024Review
- Effector-mediated subversion of proteasome activator (PA)28αβ enhances host defense against Legionella pneumophila under inflammatory and oxidative stress conditions.PLoS pathogens · 2023Article
- Intrabacterial Regulation of a Cytotoxic Effector by Its Cognate Metaeffector Promotes Legionella pneumophila Virulence.mSphere · 2023Article
- Glycosylating Effectors ofBiomolecules · 2022Review
- Pathogenicity and Virulence ofVirulence · 2021Review
- Mutational analysis reveals potential phosphorylation sites in eukaryotic elongation factor 1A that are important for its activity.FEBS letters · 2021Article
- 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
- TIP30 counteracts cardiac hypertrophy and failure by inhibiting translational elongation.EMBO molecular medicine · 2019Article
- The Binary Toxin CDT ofToxins · 2018Article
- Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.The Journal of biological chemistry · 2017Article
- Diverse mechanisms of metaeffector activity in an intracellular bacterial pathogen, Legionella pneumophila.Molecular systems biology · 2016Article
- Host-pathogen interaction profiling using self-assembling human protein arrays.Journal of proteome research · 2015Article
- Roles of Asp179 and Glu270 in ADP-Ribosylation of Actin by Clostridium perfringens Iota Toxin.PloS one · 2015Article
- Article
- Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.Nucleic acids research · 2014Article
- Release factor eRF3 mediates premature translation termination on polylysine-stalled ribosomes in Saccharomyces cerevisiae.Molecular and cellular biology · 2014Article
- Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Legionella is a pathogenic Gram-negative bacterium that can multiply inside of eukaryotic cells. It translocates numerous bacterial effector proteins into target cells to transform host phagocytes into a niche for replication. One effector of Legionella pneumophila is the glucosyltransferase Lgt1, which modifies serine 53 in mammalian elongation factor 1A (eEF1A), resulting in inhibition of protein synthesis and cell death. Here, we demonstrate that similar to mammalian cells, Lgt1 was severely toxic when produced in yeast and effectively inhibited in vitro protein synthesis. Saccharomyces cerevisiae strains, which were deleted of endogenous eEF1A but harbored a mutant eEF1A not glucosylated by Lgt1, were resistant toward the bacterial effector. In contrast, deletion of Hbs1, which is also an in vitro substrate of the glucosyltransferase, did not influence the toxic effects of Lgt1. Serial mutagenesis in yeast showed that Phe(54), Tyr(56) and Trp(58), located immediately downstream of serine 53 of eEF1A, are essential for the function of the elongation factor. Replacement of serine 53 by glutamic acid, mimicking phosphorylation, produced a non-functional eEF1A, which failed to support growth of S. cerevisiae. Our data indicate that Lgt1-induced lethal effect in yeast depends solely on eEF1A. The region of eEF1A encompassing serine 53 plays a critical role in functioning of the elongation factor.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.