Genetic control of repression of alkaline phosphatase in E. coli

Echols, Harrison; Garen, Alan; Garen, Suzanne; Torriani, Annamaria

doi:10.1016/s0022-2836(61)80055-7

Cited by 326 publications

(158 citation statements)

References 8 publications

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“…This medium and dye has been earlier utilized by Satta et al, 1979 [15]; Riccio et al, 1997 [16] and Nilgiriwala et al, 2008 [17]. The other techniques for selecting phosphatase producers are Yellow colonies through p-NPP [18], indigo blue colonies through indolyl phosphate [19] and precipitating fluorescence using 2-(5"-chloro-2"-phosphoryloxyphenyl)-4-[3H]-quinazolinone [20]. The PDP plus methyl green method is advantageous as it avoids contamination and distinguishes between excreted and cellular phosphatase.…”

Section: Discussionmentioning

confidence: 99%

Novel Organophosphate Pesticide Utilizing Alkaline Phosphatase Producing Polyextremophile Bacillus Flexus from Lake Ecosystem of North Gujarat, India

Falguni¹,

Sharma²

2014

IJIRSET

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ABSTRACT:The biodiversity of alkaline phosphatase (ALP) producing microbes from the lake ecosystem of the North Gujarat region was explored. Methyl Green dye and Phenolphthalein diphosphate supplemented MG-PDP medium screened ALP producing microbes as deep green stained cultures. The best ALP producing isolate was put through phenetic and genetic identification on the basis of morphology, biochemistry, physiology and 16S rRNA analysis. This best ALP producer proved to be catalase and oxidase positive, spore forming, noncapsulated, motile, vancomycin sensitive Gram-positive rod which gives optimum ALP production at pH 9.0, 35ºC and 0.5% NaCl concentration. Scanning Electron Micrographs revealed unique pili like bridge between bacterial cells and no flagella. N-BLAST search of the 16S rRNA sequence of the isolate (GenBank accession no JN415115) exhibited maximum similarity (98%) with Bacillus flexus. Organophosphorous Pesticide Acephate was utilized as sole Carbon source accompanied with the release of inorganic phosphate indicating its role in organophosphate pesticide bioremediation.

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Section: Discussionmentioning

confidence: 99%

Novel Organophosphate Pesticide Utilizing Alkaline Phosphatase Producing Polyextremophile Bacillus Flexus from Lake Ecosystem of North Gujarat, India

Falguni¹,

Sharma²

2014

IJIRSET

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“…Escherichia coli c 4 (a strain derived from K-10), isolated and described by Echols, Garen, Garen & Torriani (1961), was used as the source of analogueresistant strains described below. Strains resistant to 3,4-dehydroproline were isolated by plating between 108 and 109 bacteria of strain c 4 (without exposure to mutagens) on Proline uptake and analogue resistance 123 232 G/DHP agar.…”

Section: Methodsmentioning

confidence: 99%

The Activity and Specificity of the Proline Permease in Wild-type and Analogue-resistant Strains of Escherichia coli

Tristram

Neale

1968

Journal of General Microbiology

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SUMMARYThe main characteristics of the previously described proline-specific transport mechanism (permease) of Escherichia coli were confirmed in strain c4. The same permease was responsible for entry of a number of proline analogues, including 3,4-dehydroproline7 4-methyleneprolineY cis-and trans-4-chloroprolines, thiazolidine-4-carboxylic acid (thioproline) and the lower homologue, azetidine-2-carboxylic acid. These analogues also entered the cells by an exchange reaction between extracellular analogue and previously accumulated intracellular proline. Growth of the parent (c 4) strain was inhibited by 3,4-dehydroproline and azetidine-2-carboxylic acid, both of which were incorporated into cellular protein. Several classes of mutants, selected for resistance to either dehydroproline or azetidine, failed to incorporate one or both analogues into protein. Some of these mutants owed their resistance to failure to produce a functional proline permease. At least one strain, resistant to azetidine but not to dehydroproline, possessed an altered permease with little affinity for azetidine-2-carboxylic acid but still capable of transporting proline and 3,4-dehydroproline ; the permease of this strain could no longer promote exchange between intracellular proline and extracellular proline or proline analogues.

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“…As we wanted to study the pore activity in the presence of the phosphate binding protein, we could not use a phoS mutation for the construction of a strain with high levels of PhoE protein but we were dependent on a phoR mutation. However, phoR strains produce relatively little PhoE protein [30], but this problem was solved by the discovery that strain C3, carrying the phoR69 mutation and known to produce high levels of alkaline phosphatase [31], is exceptional in that it produces high levels of PhoE protein. Therefore this phoR69 allele was crossed into ompB strain CEll07 which resulted in strain CE1230, which produces PhoE protein as the only pore protein.…”

Section: Construction Of Strainsmentioning

confidence: 99%

PhoE protein pore of the outer membrane of Escherichia coli K12 is a particularly efficient channel for organic and inorganic phosphate

Korteland

Tommassen

Lugtenberg

1982

Biochimica et Biophysica Acta (BBA) - Biomembranes

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This study was undertaken to investigate the proposed in vivo pore function of PhoE protein, an Escherichia coil KI2 outer membrane protein induced by growth under phosphate limitation, and to compare it with those of the constitutive pore proteins OmpF and OmpC. Appropriate mutant strains were constructed containing only one of the proteins PhoE, OmpF or OmpC, or none of these proteins at all. By measuring rates of nutrient uptake at low solute concentrations, the proposed pore function of PhoE protein was confirmed as the presence of the protein facilitates the diffusion of Pi through the outer membrane, such that a pore protein deficient strain behaves as a K m mutant. Comparison of the rates of permeation of Pi, glycerol 3-phosphate and glucose 6-phosphate through pores formed by PhoE, OmpF and OmpC proteins shows that PhoE protein is the most effective pore in facilitating the diffusion of Pi and phosphorus-containing compounds. The three types of pores were about equally effective in facilitating the permeation of glucose and arsenate. Possible reasons for the preference for Pi and Pi-containing solutes are discussed.

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Genetic control of repression of alkaline phosphatase in E. coli

Cited by 326 publications

References 8 publications

Novel Organophosphate Pesticide Utilizing Alkaline Phosphatase Producing Polyextremophile Bacillus Flexus from Lake Ecosystem of North Gujarat, India

Novel Organophosphate Pesticide Utilizing Alkaline Phosphatase Producing Polyextremophile Bacillus Flexus from Lake Ecosystem of North Gujarat, India

The Activity and Specificity of the Proline Permease in Wild-type and Analogue-resistant Strains of Escherichia coli

PhoE protein pore of the outer membrane of Escherichia coli K12 is a particularly efficient channel for organic and inorganic phosphate

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