Protein D1 — A glucose-inducible, pore-forming protein from the outer membrane of Pseudomonas aeruginosa

Hancock, R

doi:10.1016/0378-1097(80)90079-8

Cited by 47 publications

(82 citation statements)

References 5 publications

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“…First, both synonymous mutations occur in a gene predicted to encode a permease subunit of an ABC transporter, and homologues of this transport system in P. aeruginosa and P. putida are glucose inducible and responsible for glucose uptake ( Fig. 2) [21][22][23][24] . Second, the benefits conferred are specific to glucose: neither mutation significantly affected fitness on alternate sugars (Fig.…”

Section: Resultsmentioning

confidence: 99%

Adaptive synonymous mutations in an experimentally evolved Pseudomonas fluorescens population

2014

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Conventional wisdom holds that synonymous mutations, nucleotide changes that do not alter the encoded amino acid, have no detectable effect on phenotype or fitness. However, a growing body of evidence from both comparative and experimental studies suggests otherwise. Synonymous mutations have been shown to impact gene expression, protein folding and fitness, however, direct evidence that they can be positively selected, and so contribute to adaptation, is lacking. Here we report the recovery of two beneficial synonymous single base pair changes that arose spontaneously and independently in an experimentally evolved population of Pseudomonas fluorescens. We show experimentally that these mutations increase fitness by an amount comparable to non-synonymous mutations and that the fitness increases stem from increased gene expression. These results provide unequivocal evidence that synonymous mutations can drive adaptive evolution and suggest that this class of mutation may be underappreciated as a cause of adaptation and evolutionary dynamics.

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Section: Resultsmentioning

confidence: 99%

Adaptive synonymous mutations in an experimentally evolved Pseudomonas fluorescens population

2014

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“…However, toluene did not affect the oxidative route of glucose metabolism (del Castillo & Ramos, 2007). The phosphorylative mode of glucose metabolism requires its transport inside the cell and involves: (i) an inducible outer-membrane protein (Hancock & Carey, 1980;Saravolac et al, 1991;Wylie & Worobec, 1995), (ii) an inducible periplasmic glucose-binding protein (Basu et al, 2007;Sly et al, 1993;Stinson et al, 1977) and (iii) a putative inner-membrane protein(s) (Adewoye & Worobec, 2000). So far, to our knowledge, all three components have not been reported from a single Pseudomonas strain.…”

Section: Introductionmentioning

confidence: 99%

“…In Pseudomonas, glucose uptake occurs via either oxidative (low affinity, K m 1-2 mM) or phosphorylative (high affinity, K m 8 mM) pathways (Hancock & Carey, 1980;Midgley & Dawes, 1973;. The oxidative pathway involves two different routes of glucose metabolism.…”

Section: Introductionmentioning

confidence: 99%

“…The channel-forming proteins present in the outer membrane of Gram-negative bacteria, generally termed as porins, allow diffusion of nutrients, metabolites and toxic waste across the outer membrane (Hancock & Carey, 1980;Nikaido, 2003). Porins are of two types: (i) non-specific porins which allow diffusion of substrates on the basis of mass, charge and polarity, e.g.…”

Section: Introductionmentioning

confidence: 99%

“…OmpF of E. coli (Cowan et al, 1992) or OprF of Pseudomonas aeruginosa Sugawara et al, 2006), and (ii) specific channels which show high-affinity substrate transport and often possess a binding site for a given substrate within the channel e.g. maltodextrin-specific LamB of E. coli (Benz et al, 1987), glucose-specific OprB of P. aeruginosa and P. putida (Hancock & Carey, 1980;Saravolac et al, 1991;Trias et al, 1988;, imipenem-and basic amino-acid-specific OprD (Trias & Nikaido, 1990) and phosphate-specific OprP (Hancock et al, 1982;Hancock & Benz, 1986) of P. aeruginosa. P. putida strain CSV86 (hereafter referred to as CSV86) is a soil isolate that utilizes aromatic compounds or organic acids in preference to glucose .…”

Section: Introductionmentioning

confidence: 99%

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Repression of the glucose-inducible outer-membrane protein OprB during utilization of aromatic compounds and organic acids in Pseudomonas putida CSV86

et al. 2011

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Pseudomonas putida CSV86 shows preferential utilization of aromatic compounds over glucose. Protein analysis and [ 14 C]glucose-binding studies of the outer membrane fraction of cells grown on different carbon sources revealed a 40 kDa protein that was transcriptionally induced by glucose and repressed by aromatics and succinate. Based on 2D gel electrophoresis and liquid chromatography-tandem mass spectrometry analysis, the 40 kDa protein closely resembled the porin B of P. putida KT2440 and carbohydrate-selective porin OprB of various Pseudomonas strains. The purified native protein (i) was estimated to be a homotrimer of 125 kDa with a subunit molecular mass of 40 kDa, (ii) displayed heat modifiability of electrophoretic mobility, (iii) showed channel conductance of 166 pS in 1 M KCl, (iv) permeated various sugars (mono-, di-and trisaccharides), organic acids, amino acids and aromatic compounds, and (v) harboured a glucosespecific and saturable binding site with a dissociation constant of 1.3 mM. These results identify the glucose-inducible outer-membrane protein of P. putida CSV86 as a carbohydrate-selective protein OprB. Besides modulation of intracellular glucose-metabolizing enzymes and specific glucose-binding periplasmic space protein, the repression of OprB by aromatics and organic acids, even in the presence of glucose, also contributes significantly to the strain's ability to utilize aromatics and organic acids over glucose.

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Mechanism of imipenem resistance acquired by threePseudomonas aeruginosa strains during imipenem therapy

Vurma-Rapp

Kayser

Hadorn

et al. 1990

Eur. J. Clin. Microbiol. Infect. Dis.

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Imipenem sensitive pretherapy isolates (MICs 1-2 mg/l) and the corresponding resistant posttherapy isolates (MICs 16 mg/l) of Pseudomonas aeruginosa from three patients undergoing imipenem treatment were analyzed to establish the resistance mechanism. The identity of pyocin types, serotypes, DNA restriction endonuclease profiles and plasmid profiles strongly suggested isogenicity of pre- and posttherapy isolates. The imipenem resistant posttherapy isolates showed cross-resistance only to another carbapenem, meropenem. There were neither qualitative nor quantitative differences between pre- and posttherapy isolates in beta-lactamase production. Affinity of the penicillin-binding proteins 1A, 1B, 2, 3, 4,4' and 5 for [14C]imipenem was the same in pre- and posttherapy isolates. One-dimensional and two-dimensional gel electrophoresis of outer membrane protein preparations showed diminished expression of an outer membrane protein of about 46.5 and 47.5 kilodaltons, respectively, in the posttherapy isolates. This protein had an apparent isoelectric point of about pH 5.2 in two-dimensional gel electrophoresis. Growth in proteose peptone no. 2 broth did not reduce expression of this outer membrane protein, which spoke against its identity with the outer membrane protein D1. The permeability of the outer membrane for imipenem was reduced in the posttherapy isolates, since addition of 0.5 or 0.25 of the MIC of the permeabilizing agent ethylene-diaminetetraacetate reduced the MICs of imipenem for all isolates from each patient to the same (susceptible) level. The diminished expression of one of the outer membrane proteins might be the reason for this reduced permeability.

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Protein D1 — A glucose-inducible, pore-forming protein from the outer membrane of Pseudomonas aeruginosa

Cited by 47 publications

References 5 publications

Adaptive synonymous mutations in an experimentally evolved Pseudomonas fluorescens population

Adaptive synonymous mutations in an experimentally evolved Pseudomonas fluorescens population

Repression of the glucose-inducible outer-membrane protein OprB during utilization of aromatic compounds and organic acids in Pseudomonas putida CSV86

Mechanism of imipenem resistance acquired by threePseudomonas aeruginosa strains during imipenem therapy

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