A Possible Negative Feedback Phenomenon controlling Formation of Alkaline Phosphomonoesterase in Escherichia coli

@article{Horiuchi1959APN,
  title={A Possible Negative Feedback Phenomenon controlling Formation of Alkaline Phosphomonoesterase in Escherichia coli},
  author={Tadao Horiuchi and S Horiuchi and Den'ichi Mizuno},
  journal={Nature},
  year={1959},
  volume={183},
  pages={1529-1530}
}
WE have already reported1 that in a phosphate-deficient medium the amount of ribonucleic acid in E. coli decreased remarkably, while there was an appreciable increase of deoxyribonucleic acid, protein and viable cell numbers. At the same time we also studied activities of some enzymes presumed to be related to the degradation of ribonucleic acid, for example, ribonuclease phosphodiesterase and phosphomonoesterase, and found a marked increase in that of phosphomonoesterase. This communication is… Expand
Physiological Factors in the Regulation of Alkaline Phosphatase Synthesis in Escherichia coli
  • A. Wilkins
  • Medicine, Biology
  • Journal of bacteriology
  • 1972
TLDR
Experiments with purine-requiring mutants suggest that phosphatase is induced in wild-type strains by an adenine nucleotide, and may be linked to alterations in the levels of the nucleotide pools. Expand
AN INCREASE IN ALKALINE PHOSPHATASE IN AN IN VITRO SYSTEM DERIVED FROM BACILLUS SUBTILIS.
TLDR
The present communication describes a similar observation with respect to alkaline phosphatase of B. subtilis and presents evidence concerning requirements and the effects of inhibitors, and the requirement for a supernatant fraction from a genetically competent strain is discussed. Expand
Some properties of alkaline phosphatase of Pseudomonas fluorescens.
The formation of alkaline phosphatase in a strain of Pseudomonas fluorescens was found to be induced by limiting quantities of orthophosphate in the extracellular medium. The substrate specificity ofExpand
Acid phosphatase and the growth of Escherichia coli.
Abstract 1. 1. The acid phosphatase activity of E. coli varies considerably with the conditions of growth and the physiological state of the cells. The nature and concentration of the source ofExpand
Acid phosphatases of Escherichia coli.
TLDR
Two types of acid phosphatase activity have been observed in extracts of Escherichia coli and it is suggested that these hexosephosphatases represent complexes of enzymes or multiple forms of enzymes. Expand
Purification, subunit structure and properties of two repressible phosphohydrolases of Bacillus subtilis.
TLDR
Results presented indicate that (a) the enzymes are indeed repressed in presence of excess Pi and (b) they are not structurally related and, especially do not share a common subunit. Expand
Genetic control of repression of alkaline phosphatase in E. coli.
TLDR
Results of cis-trans tests show that the constitutive alleles of the two genes are recessive in both cis and trans positions relative to the structural gene, which suggests that each regulator gene plays an essential role in the formation of a repressor for alkaline phosphatase. Expand
Reutilization of degradation products of ribosomal ribonucleic acid in Escherichia coli strain B during the phosphorus-deficient stage.
Abstract A closer investigation was carried out into the acid-soluble nucleotides of Escherichia coli B during the phosphorus-deficient stage in order to clarify the mechanism of reutilization of theExpand
The loss of the phoS periplasmic protein leads to a change in the specificity of a constitutive inorganic phosphate transport system in Escherichia coli.
TLDR
It would appear that the periplasmic phoS protein is not essential for Pi accumulation but is involved in maintaining the specificity of the PST Pi transport system. Expand
REPRESSIBLE ACID PHOSPHOMONOESTERASE AND CONSTITUTIVE PYROPHOSPHATASE OF SACCHAROMYCES MELLIS
TLDR
Saccharomyces mellis produces a nonspecific acid phosphomonoesterase (pH optimum of 5.5 to 6.0) when grown in a medium devoid of phosphate, and contains an inorganic pyrophosphatase with a pH optimum of 7.5. Expand
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