Properties of the transport systems for amino acids in Pseudomonas aeruginosa were investigated. Exogenous "4C-labeled amino acids were shown to equilibrate with the internal native amino acid pool prior to incorporation into protein. When added at low external concentrations, the majority of the amino acids examined entered the protein of the cell unaltered. The rates of amino acid transport, established at low concentrations with 18 commonly occurring amino acids, varied as much as 40-fold. The transport process became saturated at high external amino acid concentrations, was temperature-sensitive, and was inhibited by sodium azide and iodoacetamide. Intracellular to extracellular amino acid ratios of 100to 300fold were maintained during exponential growth of the population in a glucose minimal medium. When the medium became depleted of glucose, neither extracellular nor intracellular amino acids could be detected.
Kinetic studies of the transport of aromatic amino acids by Pseudomonas aeruginosa revealed the existence of two high-affinity transport systems which recognized the three aromatic amino acids. From competition data and studies on the exchange of preformed aromatic amino acid pools, the first transport system was found to be functional with phenylalanine, tyrosine, and tryptophan (in order of decreasing activity), whereas the second system was active with tryptophan, phenylalanine, and tyrosine. The two systems also transported a number of aromatic amino acid analogues but not other amino acids. Mutants defective in each of the two and in both transport systems were isolated and described. When the amino acids were added at low external concentrations to cells growing logarithmically in glucose minimal medium, the tryptophan pool very quickly became saturated. Under identical conditions, phenylalanine and tyrosine each accumulated in the intracellular pool of P. aeruginosa at a concentration which was 10 times greater than that of tryptophan.
The accumulation and behavior of various amino acids in the pool of Pseudomonas aeruginosa (ATCC 9027) were investigated. Patterns of pool formation and maintenance varied with different amino acids tested and were dependent, to a considerable extent, upon the ability of the organism to catabolize the particular amino acid. The establishment of steady-state amino acid pool levels depended upon the activity of the amino acid permease involved and upon the rate of protein synthesis. The presence of a relatively large specific amino acid pool did not affect the formation of a pool of a structurally different amino acid, and a preformed steady-state pool was not displaced by structurally unrelated amino acids. Steady-state amino acid pools decreased rapidly in the presence of inhibitors of energy metabolism and at 0 C. Steady-state internal amino acid pools were found to be in equilibrium with the corresponding external amino acid, present at low levels. A multiplicity of proline pools was demonstrated.
Hou, CYNTHIA I. (University of British Columbia, Vancouver, B.C., Canada), AuDRnEY F. GRONLUND, AND J. J. R. CAMPBELL. Influence of phosphate starvation on cultures of Pseudomonas aeruginosa. J. Bacteriol. 92:851-855. 1966.-The changes occurring in Pseudomonas aeruginosa during phosphate starvation in a phosphatedeficient medium were assessed by measuring alterations in optical density, viablecell count, chemical composition, and ribosome patterns. After a 24-hr period of starvation, optical density, protein, and deoxyribonucleic acid per milliliter of culture increased, whereas ribonucleic acid decreased. Extensive ribosomal degradation was apparent from sucrose density gradient centrifugation patterns. The induction of an alkaline phosphomonoesterase during phosphate starvation was observed. A linear response of phosphate-starved cells to low levels of phosphate supplied exogenously was evident from optical-density measurements, and a threshold requirement for phosphate analogous to the "energy of maintenance" was not detected.
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