ArticleJournal of bacteriology1994
Overexpression of algE in Escherichia coli: subcellular localization, purification, and ion channel properties.
Article in Journal of bacteriology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 85 citations in OpenAlex.
- AVaccines · 2021Article
- Bioengineering a bacterial pathogen to assemble its own particulate vaccine capable of inducing cellular immunity.Scientific reports · 2017Article
- Bacterial exopolysaccharides: biosynthesis pathways and engineering strategies.Frontiers in microbiology · 2015Review
- A conformational landscape for alginate secretion across the outer membrane of Pseudomonas aeruginosa.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Microbial alginate production, modification and its applications.Microbial biotechnology · 2013Review
- Insights into the assembly of the alginate biosynthesis machinery in Pseudomonas aeruginosa.Applied and environmental microbiology · 2013Article
- Article
- Structural basis for alginate secretion across the bacterial outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Biosynthesis of the Pseudomonas aeruginosa Extracellular Polysaccharides, Alginate, Pel, and Psl.Frontiers in microbiology · 2011Article
- Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Membrane topology of outer membrane protein AlgE, which is required for alginate production in Pseudomonas aeruginosa.Applied and environmental microbiology · 2010Article
- AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin.Structure (London, England : 1993) · 2010Article
- Analysis of lipid export in hydrocarbonoclastic bacteria of the genus Alcanivorax: identification of lipid export-negative mutants of Alcanivorax borkumensis SK2 and Alcanivorax jadensis T9.Journal of bacteriology · 2010Article
- Expression, refolding, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgE.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- MucR, a novel membrane-associated regulator of alginate biosynthesis in Pseudomonas aeruginosa.Applied and environmental microbiology · 2009Article
- Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization.Microbiology (Reading, England) · 2008Article
- Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas fluorescens AlgK.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- Genetics of bacterial alginate: alginate genes distribution, organization and biosynthesis in bacteria.Current genomics · 2007Article
- Identification and characterization of an Azotobacter vinelandii type I secretion system responsible for export of the AlgE-type mannuronan C-5-epimerases.Journal of bacteriology · 2006Article
- Pseudomonas aeruginosa C5-mannuronan epimerase: steady-state kinetics and characterization of the product.Biochemistry · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alginate-producing (mucoid) strains of Pseudomonas aeruginosa possess a 54-kDa outer membrane (OM) protein (AlgE) which is missing in nonmucoid bacteria. The coding region of the algE gene from mucoid P. aeruginosa CF3/M1 was subcloned in the expression vector pT7-7 and expressed in Escherichia coli. The level of expression of recombinant AlgE was seven times higher than that of the native protein in P. aeruginosa. Recombinant AlgE was found mainly in the OM. A putative precursor protein (56 kDa) of AlgE could be immunologically detected in the cytoplasmic membrane (CM). Surface exposition of AlgE in the OM of E. coli was indicated by labeling lysine residues with N-hydroxysuccinimide-biotin. Secondary-structure analysis suggested that AlgE is anchored in the OM by 18 membrane-spanning beta-strands, probably forming a beta-barrel. Recombinant AlgE was purified, and isoelectric focusing revealed a pI of 4.4. Recombinant AlgE was spontaneously incorporated into planar lipid bilayers, forming ion channels with a single-channel conductance of 0.76 nS in 1 M KCl and a mean lifetime of 0.7 ms. Single-channel current measurements in the presence of other salts as well as reversal potential measurements in salt gradients revealed that the AlgE channel was strongly anion selective. For chloride ions, a weak binding constant (Km = 0.75 M) was calculated, suggesting that AlgE might constitute an ion channel specific for another particular anion, e.g., polymannuronic acid, which is a precursor of alginate. Consistent with this idea, the open-state probability of the channel decreased when GDP-mannuronic acid was added. The AlgE channel was inactivated when membrane voltages higher than +85 mV were applied. The electrophysiological characteristics of AlgE, including its rectifying properties, are quite different from those of typical porins.
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