ArticleScientific reports2016
E. coli metabolic protein aldehyde-alcohol dehydrogenase-E binds to the ribosome: a unique moonlighting action revealed.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Differentiating commensal and disease-associatedFrontiers in veterinary science · 2026Article
- Role of Ribosomal Protein bS1 in Orthogonal mRNA Start Codon Selection.Biochemistry · 2025Article
- The Beak of Eukaryotic Ribosomes: Life, Work and Miracles.Biomolecules · 2024Review
- Phylogenetic and functional diversity of aldehyde-alcohol dehydrogenases in microalgae.Plant molecular biology · 2021Article
- AcrR and Rex Control Mannitol and Sorbitol Utilization through Their Cross-Regulation of Aldehyde-Alcohol Dehydrogenase (AdhE) in Lactobacillus plantarum.Applied and environmental microbiology · 2019Article
- Endogenous rRNA Sequence Variation Can Regulate Stress Response Gene Expression and Phenotype.Cell reports · 2018Article
- Adaptive modulation of antibiotic resistance through intragenomic coevolution.Nature ecology & evolution · 2017Article
- Concerted Up-regulation of Aldehyde/Alcohol Dehydrogenase (ADHE) and Starch inThe Journal of biological chemistry · 2017Article
- Diversity and Evolutionary Analysis of Iron-Containing (Type-III) Alcohol Dehydrogenases in Eukaryotes.PloS one · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is becoming increasingly evident that a high degree of regulation is involved in the protein synthesis machinery entailing more interacting regulatory factors. A multitude of proteins have been identified recently which show regulatory function upon binding to the ribosome. Here, we identify tight association of a metabolic protein aldehyde-alcohol dehydrogenase E (AdhE) with the E. coli 70S ribosome isolated from cell extract under low salt wash conditions. Cryo-EM reconstruction of the ribosome sample allows us to localize its position on the head of the small subunit, near the mRNA entrance. Our study demonstrates substantial RNA unwinding activity of AdhE which can account for the ability of ribosome to translate through downstream of at least certain mRNA helices. Thus far, in E. coli, no ribosome-associated factor has been identified that shows downstream mRNA helicase activity. Additionally, the cryo-EM map reveals interaction of another extracellular protein, outer membrane protein C (OmpC), with the ribosome at the peripheral solvent side of the 50S subunit. Our result also provides important insight into plausible functional role of OmpC upon ribosome binding. Visualization of the ribosome purified directly from the cell lysate unveils for the first time interactions of additional regulatory proteins with the ribosome.
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