ArticleJournal of bacteriology2006
Role of the Pseudomonas aeruginosa PlcH Tat signal peptide in protein secretion, transcription, and cross-species Tat secretion system compatibility.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- A genome-wide screen inJournal of bacteriology · 2026Article
- Sphingosine induction of theJournal of bacteriology · 2024Article
- Engineered Sucrose Metabolism Improves the Smut Disease Suppression Potency of Pseudomonas sp. ST4.Applied and environmental microbiology · 2023Article
- Phospholipase C: underrated players in microbial infections.Frontiers in cellular and infection microbiology · 2023Review
- Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase.FEBS open bio · 2021Review
- TatC-dependent translocation of pyoverdine is responsible for the microbial growth suppression.Journal of microbiology (Seoul, Korea) · 2016Article
- Membrane Association and Catabolite Repression of the Sulfolobus solfataricus α-Amylase.Microorganisms · 2015Article
- Identification and evaluation of twin-arginine translocase inhibitors.Antimicrobial agents and chemotherapy · 2012Article
- Contribution of Phe-7 to Tat-dependent export of β-lactamase in Xanthomonas campestris.Antimicrobial agents and chemotherapy · 2012Article
- Discovery of an operon that participates in agmatine metabolism and regulates biofilm formation in Pseudomonas aeruginosa.Molecular microbiology · 2010Article
- Tat pathway-mediated translocation of the sec pathway substrate protein MexA, an inner membrane component of the MexAB-OprM xenobiotic extrusion pump in Pseudomonas aeruginosa.Antimicrobial agents and chemotherapy · 2010Article
- A complex extracellular sphingomyelinase of Pseudomonas aeruginosa inhibits angiogenesis by selective cytotoxicity to endothelial cells.PLoS pathogens · 2009Article
- Tetradecyltrimethylammonium inhibits Pseudomonas aeruginosa hemolytic phospholipase C induced by choline.Current microbiology · 2007Article
- Conservation and variation between Rhodobacter capsulatus and Escherichia coli Tat systems.Journal of bacteriology · 2006Article
- Formation of functional Tat translocases from heterologous components.BMC microbiology · 2006Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The secretion of PlcH and its homolog PlcN of Pseudomonas aeruginosa through the inner membrane depends upon a functional twin arginine translocase (Tat) system and a Tat signal sequence. Conserved twin arginine (Arg) residues within the Tat signal sequence consensus motif (S/TRRxFLK) are considered essential for the secretion of Tat substrates, but some exceptions (e.g., Lys and Arg) to the twin Arg residues in this motif have been noted. The roles of all three Arg residues within the PlcH RRRTFLK consensus motif were examined. Data are presented which indicate that Arg-9 and Arg-10 are essential for PlcH secretion across the inner membrane, but the mutation of Arg-8 (e.g., to Ala or Ser) had no observable effect on the localization of PlcH. In the signal sequence of PlcH and in all of its homologs in other bacteria, there are basic amino acid residues (Arg, Lys, and Gln) immediately adjacent to the signal peptidase cleavage site (Ala-X-Ala) that are not seen in Sec-dependent signal sequences. The mutation of these basic residues to Ala caused slightly decreased levels of extracellular PlcH, but normal localization was still observed. Deletion of the entire Tat signal sequence of PlcH not only resulted in the absence of detectable extracellular PlcH activity and protein but also caused a substantial decrease in the detectable level of plcH mRNA. Finally, data are presented which indicate that P. aeruginosa PlcH exhibits cross-species compatibility with the Escherichia coli Tat secretion machinery, but only when the E. coli Tat machinery is expressed in a P. aeruginosa host.
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