ArticleJournal of bacteriology2011
Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all gram-negative bacteria.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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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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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.
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Who cites it
39 citing papers in PubMed, 60 citations in OpenAlex.
- LpxC activity regulation: An emerging paradigm for controlling lipopolysaccharide synthesis.Trends in microbiology · 2026Article
- Protein-Protein Interactions Between Peptidoglycan, Lipopolysaccharide, and Phospholipid Biosynthesis Enzymes in Escherichia coli.Chembiochem : a European journal of chemical biology · 2026Article
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- Structural plasticity of the membrane-bound protein degradation assembly supports bacterial adaptation to stress.Cell reports · 2026Article
- Identifying Modulators of the Post-Antibiotic Effect.ACS infectious diseases · 2025Article
- Structural Plasticity of the Membrane-Bound Protein Degradation Assembly Supports Bacterial Adaptation to Stress.bioRxiv : the preprint server for biology · 2025Article
- Co-ordinated assembly of the multilayered cell envelope of Gram-negative bacteria.Current opinion in microbiology · 2024Review
- Signaling through theJournal of bacteriology · 2024Article
- Article
- Unveiling therapeutic efficacy of extract and multi-targeting phytocompounds fromRSC advances · 2024Article
- Article
- Regulated Expression ofInternational journal of molecular sciences · 2022Article
- Degron-mediated proteolysis of CrhR-like DEAD-box RNA helicases in cyanobacteria.The Journal of biological chemistry · 2022Article
- Checkpoints That Regulate Balanced Biosynthesis of Lipopolysaccharide and Its Essentiality inInternational journal of molecular sciences · 2021Review
- Impact of Target Turnover on the Translation of Drug-Target Residence Time to Time-Dependent Antibacterial Activity.ACS infectious diseases · 2021Article
- Border Control: Regulating LPS Biogenesis.Trends in microbiology · 2021Review
- Essential Genes ofFrontiers in microbiology · 2021Article
- Regulation of the First Committed Step in Lipopolysaccharide Biosynthesis Catalyzed by LpxC Requires the Essential Protein LapC (YejM) and HslVU Protease.International journal of molecular sciences · 2020Article
- The essential inner membrane protein YejM is a metalloenzyme.Scientific reports · 2020Article
- Heat-shock proteases promote survival ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the essential function of lipopolysaccharides (LPS) in Gram-negative bacteria, it is largely unknown how the exact amount of this molecule in the outer membrane is controlled. The first committed step in LPS biosynthesis is catalyzed by the LpxC enzyme. In Escherichia coli, the cellular concentration of LpxC is adjusted by the only essential protease in this organism, the membrane-anchored metalloprotease FtsH. Turnover of E. coli LpxC requires a length- and sequence-specific C-terminal degradation signal. LpxC proteins from Salmonella, Yersinia, and Vibrio species carry similar C-terminal ends and, like the E. coli enzyme, were degraded by FtsH. Although LpxC proteins are highly conserved in Gram-negative bacteria, there are striking differences in their C termini. The Aquifex aeolicus enzyme, which is devoid of the C-terminal extension, was stable in E. coli, whereas LpxC from the alphaproteobacteria Agrobacterium tumefaciens and Rhodobacter capsulatus was degraded by the Lon protease. Proteolysis of the A. tumefaciens protein required the C-terminal end of LpxC. High stability of Pseudomonas aeruginosa LpxC in E. coli and P. aeruginosa suggested that Pseudomonas uses a proteolysis-independent strategy to control its LPS content. The differences in LpxC turnover along with previously reported differences in susceptibility against antimicrobial compounds have important implications for the potential of LpxC as a drug target.
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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.