ArticlePloS one2014
The MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coli.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Filamentation-driven peripheral clustering of the inducible lysine decarboxylase is crucial for E. coli acid stress response.Communications biology · 2025Article
- Insertion of the FeFEBS letters · 2025Article
- MoxR effects as an ATPase on anti-stress and pathogenicity of Riemerella anatipestifer.Veterinary research · 2025Article
- Structural modeling and biochemical characterization of MSMEG_0748, a MoxR ATPase fromComputational and structural biotechnology journal · 2025Article
- The Phylogeny and Metabolic Potentials of an Aromatics-DegradingMicroorganisms · 2024Article
- From genome to evolution: investigating type II methylotrophs using a pangenomic analysis.mSystems · 2024Article
- Phylogenomic discernments into Anaerolineaceae thermal adaptations and the proposal of a candidate genusFrontiers in microbiology · 2024Article
- Translation Fidelity and Respiration Deficits in CLPP-Deficient Tissues: Mechanistic Insights from Mitochondrial Complexome Profiling.International journal of molecular sciences · 2023Article
- RavA-ViaA antibiotic response is linked to Cpx and Zra2 envelope stress systems inMicrobiology spectrum · 2023Article
- Article
- The Cytotoxic Mycobacteriophage Protein Phaedrus gp82 Interacts with and Modulates the Activity of the Host ATPase, MoxR.Journal of molecular biology · 2023Article
- The RavA-ViaA chaperone complex modulates bacterial persistence through its association with the fumarate reductase enzyme.The Journal of biological chemistry · 2023Article
- Article
- The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane.Nature communications · 2022Article
- Article
- Mutations in respiratory complex I promote antibiotic persistence through alterations in intracellular acidity and protein synthesis.Nature communications · 2022Article
- Amikacin and bacteriophage treatment modulates outer membrane proteins composition in Proteus mirabilis biofilm.Scientific reports · 2021Article
- Supramolecular assembly of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.Communications biology · 2020Article
- Adaptive Laboratory Evolution of Antibiotic Resistance Using Different Selection Regimes Lead to Similar Phenotypes and Genotypes.Frontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
MoxR ATPases are widespread throughout bacteria and archaea. The experimental evidence to date suggests that these proteins have chaperone-like roles in facilitating the maturation of dedicated protein complexes that are functionally diverse. In Escherichia coli, the MoxR ATPase RavA and its putative cofactor ViaA are found to exist in early stationary-phase cells at 37 °C at low levels of about 350 and 90 molecules per cell, respectively. Both proteins are predominantly localized to the cytoplasm, but ViaA was also unexpectedly found to localize to the cell membrane. Whole genome microarrays and synthetic lethality studies both indicated that RavA-ViaA are genetically linked to Fe-S cluster assembly and specific respiratory pathways. Systematic analysis of mutant strains of ravA and viaA indicated that RavA-ViaA sensitizes cells to sublethal concentrations of aminoglycosides. Furthermore, this effect was dependent on RavA's ATPase activity, and on the presence of specific subunits of NADH:ubiquinone oxidoreductase I (Nuo Complex, or Complex I). Importantly, both RavA and ViaA were found to physically interact with specific Nuo subunits. We propose that RavA-ViaA facilitate the maturation of the Nuo complex.
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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.