ArticleThe Journal of biological chemistry2012
Elongation factor G is a critical target during oxidative damage to the translation system of Escherichia coli.
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 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Triple Threat: Elucidating Evolution Under Antibiotic, Metal, and Phage Pressure inEcology and evolution · 2026Article
- Droplet-based high-throughput single microbe RNA sequencing by smRandom-seq.Nature communications · 2023Article
- Chloroplast ROS and stress signaling.Plant communications · 2022Review
- Comparative Proteomic Analysis of Psychrophilic vs. Mesophilic Bacterial Species Reveals Different Strategies to Achieve Temperature Adaptation.Frontiers in microbiology · 2022Article
- Glycinebetaine mitigated the photoinhibition of photosystem II at high temperature in transgenic tomato plants.Photosynthesis research · 2021Article
- Antimicrobial Mechanism and Identification of the Proteins Mediated by Extracts fromACS omega · 2020Article
- Oxidation of a Cysteine Residue in Elongation Factor EF-Tu Reversibly Inhibits Translation in the Cyanobacterium Synechocystis sp. PCC 6803.The Journal of biological chemistry · 2016Article
- The role of protein modifications in senescence of freeze-dried Acetobacter senegalensis during storage.Microbial cell factories · 2014Article
- Expression of a highly active catalase VktA in the cyanobacterium Synechococcus elongatus PCC 7942 alleviates the photoinhibition of photosystem II.Photosynthesis research · 2013Article
- Thiourea, a ROS scavenger, regulates source-to-sink relationship to enhance crop yield and oil content in Brassica juncea (L.).PloS one · 2013Article
- Inhibition of Cyanobacterial Growth on a Municipal Wastewater Sidestream Is Impacted by Temperature.mSphereArticle
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elongation factor G (EF-G), a key protein in translational elongation, is known to be particularly susceptible to oxidation in Escherichia coli. However, neither the mechanism of the oxidation of EF-G nor the influence of its oxidation on translation is fully understood. In the present study, we investigated the effects of oxidants on the chemical properties and function of EF-G using a translation system in vitro derived from E. coli. Treatment of EF-G with 0.5 mM H(2)O(2) resulted in the complete loss of translational activity. The inactivation of EF-G by H(2)O(2) was attributable to the oxidation of two specific cysteine residues, namely, Cys(114) and Cys(266), and subsequent formation of an intramolecular disulfide bond. Replacement of Cys(114) by serine rendered EF-G insensitive to oxidation and inactivation by H(2)O(2). Furthermore, generation of the translation system in vitro with the mutated EF-G protected the entire translation system from oxidation, suggesting that EF-G might be a primary target of oxidation within the translation system. Oxidized EF-G was reactivated via reduction of the disulfide bond by thioredoxin, a ubiquitous protein that mediates dithiol-disulfide exchange. Our observations indicate that the translational machinery in E. coli is regulated, in part, by the redox state of EF-G, which might depend on the balance between the supply of reducing power and the degree of oxidative stress.
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