The effect of inorganic phosphate on cyclic adenosine 3′, 5′-monophosphate in streptomycin-producing cultures of <i>Streptomyces griseus</i>

Terry, J. M.; Springham, Derek

doi:10.1139/m81-162

Cited by 12 publications

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“…Furthermore exogenous cAMP overcomes the phosphate inhibitiion of turimycin biosynthesis (Gersch, 1979). In the case of S. griseus the results are less cleareut and no direct relationship between antibiotic production and intracellular cAMP level has been observed (Terry, 1981).…”

Section: Introductionmentioning

confidence: 99%

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Relationships between growth, cyclic amp and tylosin production in two mutants of Streptomyces fradiae

1982

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Section: Introductionmentioning

confidence: 99%

“…Samples of the cultures were centrifuged at 8000 xg at 4°C for 5 min. The intracellular cAMP was extracted as reported by Terry (1981) and determined in duplicate at 3 differen£ dilutions with the RIA Kit from NEN.…”

Section: Introductionmentioning

confidence: 99%

Relationships between growth, cyclic amp and tylosin production in two mutants of Streptomyces fradiae

1982

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“…Evidence has been obtained which links cyclic AMP to control of a variety of metabolic processes in Streptomyces hygroscopicus including germination [3,4], growth [5,6] and phosphate inhibition of secondary metabolism [7]. The occurrence of cyclic AMP has also been described in other Streptomyces [8,9]. Both in S. hyg, roscopicus [5] and S. griseus [8] cyclic AMP levels were found to be high during growth phase and declined at the onset of stationary phase indicating that antibiotic synthesis is not regulated by catabolite repression of the E. coli-type [10,11].…”

Section: Introductionmentioning

confidence: 99%

Dependence of turimycin biosynthesis on different substrates and its relationship to cyclic AMP levels of Streptomyces hygroscopicus

Gersch¹

1982

FEMS Microbiology Letters

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“…1 phate release in turimycin fermentation, leading to a partial repression of the dephosphorylating enzyme activities. GERSCH et al 1978, GERSCH 1980, TERRY and SPRINGHAM 1981. In turimycin-producing strains of S. hygroscopicus and in S. griseus the intracellular levels of cyclic AMP were found to fall at the onset of secondary metabolism.…”

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confidence: 99%

Parallel regulation of cAMP phosphodiesterase and phosphatase activities in turimycin fermentations

Römer

Müller

1983

J of Basic Microbiology

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Phosphate limitation induces the turimycin biosyntliesis as well as the CAMP phosphodiesterase and phosphatase. The results are discussed in connection with the observation of general high activities of dephosphorylating enzymes and low concentrations of phosphorylated intermediates under conditions of phosphate limitation and secondary product biosynthesis, respectively.Although antibiotics are the most important group of secondary metabolites ex ploited by man, relatively little is known about the regulation of their biosynthesisin technical fermentations. But it is well-known that inorganic phosphate exhibits a marked inhibitory effect on a wide range of secondary metabolic processes (WEIN-BERG 1970). To prevent inhibition of antibiotic production many antibiotic fermentations must be conducted in the presence of inorganic phosphate levels suboptimal for growth (MARTIN and DEMAIN 1980). The biosynthesis of the macrolide antibiotic turimycin only starts after phosphate limitation (GERSCH et al. 1978). Additionally, a drastic increase of dephosphorylating enzymes of different type has been found during the production phase of turimycin, e. g. phosphatases active a t different p H (MULLER et al. 1983), ATPase, and thiamine pyrophosphatase (unpublished results).In view of the now well-established presence of cyclic AMP in antibiotic fermentations i t is of interest whether the CAMP-hydrolyzing enzyme cAMP phosphodiesterase is regulated parallel to other dephosphorylating enzymes such as phosphatases. Our investigation was undertaken to determine if any changes of cyclic AMP and its hydrolyzing enzyme occur during the fermentation process of turimycin. The results obtained are seen in relation to the sequential processes of phosphate limitation and of phosphate release from complex phosphate-containing medium constituents. The significance of phosphate release was found to be a modification of the process kinetics and the activities of dephosphorylating enzymes, especially in later phases of the fermentation (MULLER et al. 1981 a and b, 1983).Over a 102-hr period in two independent fermentations intracellular and extracellular enzymatic activities were measured. Both different phosphatases and CAMP phosphodiesterase indicate characteristic alterations in their activities in dependence on the age of the culture, as can be seen in Fig. 1A. The conditions of cultivation and the medium containing glucose, potato starch, and soya meal are described by MUL-LER et al. (1981a and b).The determination of CAMP phosphodiesterase activity (2.1 ,UM initial substrate concentration) utilizing the radioisotope method of THOMPSON and APPLEMAN (1971) shows a maximum decrease in activity within the 20th hr. Later we found a moderate

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The effect of inorganic phosphate on cyclic adenosine 3′, 5′-monophosphate in streptomycin-producing cultures of Streptomyces griseus

Cited by 12 publications

References 0 publications

Relationships between growth, cyclic amp and tylosin production in two mutants of Streptomyces fradiae

Relationships between growth, cyclic amp and tylosin production in two mutants of Streptomyces fradiae

Dependence of turimycin biosynthesis on different substrates and its relationship to cyclic AMP levels of Streptomyces hygroscopicus

Parallel regulation of cAMP phosphodiesterase and phosphatase activities in turimycin fermentations

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