ArticleMicrobiologyOpen2014
Organization of the Escherichia coli aerobic enzyme complexes of oxidative phosphorylation in dynamic domains within the cytoplasmic membrane.
Article in MicrobiologyOpen, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- Manipulation of the nucleotide pool in human, bacterial and plant immunity.Nature reviews. Immunology · 2026Review
- Cellular function of the GndA microprotein during heat shock.bioRxiv : the preprint server for biology · 2025Article
- Article
- Hypothesis: bacteria live on the edge of phase transitions with a cell cycle regulated by a water-clock.Theory in biosciences = Theorie in den Biowissenschaften · 2024Article
- Phages reconstitute NADNature · 2024Article
- Quantitative proteomic analysis provides insight into the survival mechanism ofCurrent research in food science · 2022Article
- Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics.International journal of molecular sciences · 2021Review
- Article
- Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes.Chemical reviews · 2021Review
- Supramolecular assembly of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- The archaeal-bacterial lipid divide, could a distinct lateral proton route hold the answer?Biology direct · 2020Article
- Clustering as a Means To Control Nitrate Respiration Efficiency and Toxicity in Escherichia coli.mBio · 2019Article
- A Mechanism of Modulating the Direction of Flagellar Rotation in Bacteria by Fumarate and Fumarate Reductase.Journal of molecular biology · 2019Article
- Substrate-dependent cluster density dynamics of Corynebacterium glutamicum phosphotransferase system permeases.Molecular microbiology · 2019Article
- Lipid-mediated Protein-protein Interactions Modulate Respiration-driven ATP Synthesis.Scientific reports · 2016Article
- Biotechnological production of limonene in microorganisms.Applied microbiology and biotechnology · 2016Review
- Different Functions of Phylogenetically Distinct Bacterial Complex I Isozymes.Journal of bacteriology · 2016Article
- The membrane: transertion as an organizing principle in membrane heterogeneity.Frontiers in microbiology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli cytoplasmic membrane contains the enzyme complexes of oxidative phosphorylation (OXPHOS). Not much is known about their supramolecular organization and their dynamics within the membrane in this model organism. In mitochondria and other bacteria, it was demonstrated by nondenaturing electrophoretic methods and electron microscopy that the OXPHOS complexes are organized in so-called supercomplexes, stable assemblies with a defined number of the individual enzyme complexes. To investigate the organization of the E. coli enzyme complexes of aerobic OXPHOS in vivo, we established fluorescent protein fusions of the NADH:ubiquinone oxidoreductase, the succinate:ubiquinone oxidoreductase, the cytochrome bd-I, and the cytochrome bo3 terminal oxidases, and the FoF1 ATP-synthase. The fusions were integrated in the chromosome to prevent artifacts caused by protein overproduction. Biochemical analysis revealed that all modified complexes were fully assembled, active, and stable. The distribution of the OXPHOS complexes in living cells was determined using total internal reflection fluorescence microscopy. The dynamics within the membrane were detected by fluorescence recovery after photobleaching. All aerobic OXPHOS complexes showed an uneven distribution in large mobile patches within the E. coli cytoplasmic membrane. It is discussed whether the individual OXPHOS complexes are organized as clustered individual complexes, here called "segrazones."
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.