ArticleGenome research2005
Genome-wide identification of Pseudomonas aeruginosa exported proteins using a consensus computational strategy combined with a laboratory-based PhoA fusion screen.
Article in Genome research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 118 citations in OpenAlex.
- Article
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- Systems-level exploitation of OxyR regulon unravels a potential antibacterial target in Pseudomonas aeruginosa.Communications biology · 2025Article
- Deciphering the enigmatic PilY1 ofBiochemistry and biophysics reports · 2024Article
- A PQS-Cleaving Quorum Quenching Enzyme Targets Extracellular Membrane Vesicles ofBiomolecules · 2022Article
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- Cell Envelope Stress Response in Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022Article
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- Quantitating denaturation by formic acid: imperfect repeats are essential to the stability of the functional amyloid protein FapC.The Journal of biological chemistry · 2020Article
- Deciphering the Role of Multiple Thioredoxin Fold Proteins ofInternational journal of molecular sciences · 2020Article
- Gingimaps: Protein Localization in the Oral PathogenMicrobiology and molecular biology reviews : MMBR · 2020Review
- Pseudomonas aeruginosa Requires the DNA-Specific Endonuclease EndA To Degrade Extracellular Genomic DNA To Disperse from the Biofilm.Journal of bacteriology · 2019Article
- Proteome profiling of Pseudomonas aeruginosa PAO1 identifies novel responders to copper stress.BMC microbiology · 2019Article
- Article
- Genome wide identification and experimental validation of Pseudomonas aeruginosa Tat substrates.Scientific reports · 2018Article
- The EXIT Strategy: an Approach for Identifying Bacterial Proteins Exported during Host Infection.mBio · 2017Article
- PilY1 PromotesFrontiers in cellular and infection microbiology · 2017Article
- Using Chemical Probes to Assess the Feasibility of Targeting SecA for Developing Antimicrobial Agents against Gram-Negative Bacteria.ChemMedChem · 2016Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Gram-negative pathogen Pseudomonas aeruginosa encodes multiple protein export systems, the substrates of which contain export signals such as N-terminal signal peptides. Here we report the first genome-wide computational and laboratory screen for N-terminal signal peptides in this important opportunistic pathogen. The computational identification of signal peptides was based on a consensus between multiple predictive tools and showed that 38% of the P. aeruginosa PAO1 proteome was predicted to encode exported proteins, most of which utilize cleavable type I signal peptides or uncleavable transmembrane helices. In addition, known and novel lipoproteins (type II), twin arginine transporter (TAT), and prepilin peptidase substrates (type IV) were also identified. A laboratory-based screen using the alkaline phosphatase (PhoA) fusion method was then used to test our predictions. In total, 310 nonredundant PhoA fusions were successfully identified, 296 of which possess a predicted export signal. Analysis of the PhoA fusion proteins lacking an export signal revealed that three proteins have alternate translation start sites that encode signal peptides, two proteins may use an unknown export signal, and the remaining nine proteins are likely cytoplasmic proteins and represent false positives associated with the PhoA screen. Our approach to identify exported proteins illustrates how computational and laboratory-based methods are complementary, where computational analyses provide a large number of accurate predictions while laboratory methods both confirm predictions and reveal unique cases meriting further analysis.
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