ArticleJournal of bacteriology2008
Novel inner membrane retention signals in Pseudomonas aeruginosa lipoproteins.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 77 citations in OpenAlex.
- A surface-exposed cardiolipin synthase provides an unexpected paradigm for maintaining the Gram-negative outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
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- The Type II Secretion System Utilizes AsmA-like Protein GspN to Facilitate Transport of Lipoproteins to the Cell Surface inbioRxiv : the preprint server for biology · 2025Article
- Mechanical stability of individual bacterial cells under different osmotic pressure conditions: a nanoindentation study ofBeilstein journal of nanotechnology · 2025Article
- Structural characterization of lytic transglycosylase MltD of Pseudomonas aeruginosa, a target for the natural product bulgecin A.International journal of biological macromolecules · 2024Article
- Identification and characterization of an abundant lipoprotein from Methylacidiphilum fumariolicum SolV.Archives of microbiology · 2023Article
- Identification of an Essential LolD-Like Protein in Helicobacter pylori.Journal of bacteriology · 2023Article
- Article
- Cell Envelope Stress Response in Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022Article
- Direct and Indirect Interactions Promote Complexes of the Lipoprotein LbcA, the CtpA Protease and Its Substrates, and Other Cell Wall Proteins in Pseudomonas aeruginosa.Journal of bacteriology · 2021Article
- Disorder is a critical component of lipoprotein sorting in Gram-negative bacteria.Nature chemical biology · 2021Article
- Mechanism of LolCDE as a molecular extruder of bacterial triacylated lipoproteins.Nature communications · 2021Article
- Bacterial Lipoprotein Posttranslational Modifications. New Insights and Opportunities for Antibiotic and Vaccine Development.Frontiers in microbiology · 2021Review
- Structural characterization of PaFkbA: A periplasmic chaperone fromComputational and structural biotechnology journal · 2021Article
- Article
- Lipoproteins and Their Trafficking to the Outer Membrane.EcoSal Plus · 2019Review
- The Pathogenic Neisseria Use a Streamlined Set of Peptidoglycan Degradation Proteins for Peptidoglycan Remodeling, Recycling, and Toxic Fragment Release.Frontiers in microbiology · 2019Review
- Aspartate tightens the anchoring of staphylococcal lipoproteins to the cytoplasmic membrane.MicrobiologyOpen · 2017Article
- Lytic transglycosylases: concinnity in concision of the bacterial cell wall.Critical reviews in biochemistry and molecular biology · 2017Review
- Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.Journal of bacteriology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ultimate membrane localization and function of most of the 185 predicted Pseudomonas aeruginosa PAO1 lipoproteins remain unknown. We constructed a fluorescent lipoprotein, CSFP(OmlA)-ChFP, by fusing the signal peptide and the first four amino acids of the P. aeruginosa outer membrane lipoprotein OmlA to the monomeric red fluorescent protein mCherry (ChFP). When cells were plasmolyzed with 0.5 M NaCl, the inner membrane separated from the outer membrane and formed plasmolysis bays. This permits the direct observation of fluorescence in either the outer or inner membrane. CSFP(OmlA)-ChFP was shown to localize in the outer membrane by fluorescence microscopy and immunoblotting analysis of inner and outer membrane fractions. The site-directed substitution of the amino acids at positions +2, +3, and +4 in CSFP(OmlA)-ChFP was performed to test the effects on lipoprotein localization of a series of amino acid sequences selected from a panel of predicted lipoproteins. We confirmed Asp(+2) and Lys(+3) Ser(+4) function as inner membrane retention signals and identified four novel inner membrane retention signals: CK(+2) V(+3) E(+4), CG(+2) G(+3) G(+4), CG(+2) D(+3) D(+4), and CQ(+2) G(+3) S(+4). These inner membrane retention signals are found in 5% of the 185 predicted P. aeruginosa lipoproteins. Full-length chimeras of predicted lipoproteins PA4370 and PA3262 fused to mCherry were shown to reside in the inner membrane and showed a nonuniform or patchy distribution in the membrane. The optical sectioning of cells producing PA4370(CGDD)-ChFP and PA3262(CDSQ)-ChFP by confocal microscopy improved the resolution and indicated a helix-like localization pattern in the inner membrane. The method described here permits the in situ visualization of lipoprotein localization and should work equally well for other membrane-associated proteins.
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Registered trials
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