REGULATORY PATTERNS IN PUTRESCINE BIOSYNTHESIS IN <i>ESCHERICHIA COLI</i>

Morris, David R.; Wu, Wen‐guey; Applebaum, Deborah M.; Koffron, Kara L.

doi:10.1111/j.1749-6632.1970.tb39402.x

Cited by 62 publications

(49 citation statements)

References 22 publications

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“…In contrast, F,MeOm does not reduce the infectivity of 7: cruzi trypomastigotes in vitro, suggesting that invasion of mammalian cells is independent of the ornithine decarboxylase pathway in this non-dividing stage of the parasite life cycle [9]. However, further work by Kierszenbaum et al [lo, 111 has provided evidence that polyamines in 7: cruzi trypomastigotes are synthesised to some extent via arginine decarboxylase, an enzyme found normally in bacteria and higher plants [12,131. Consistent with these data, a high concentration (50 mM) of the arginine decarboxylase inhibitor DL-adifluoromethylarginine (F,MeArg) was reported to interfere with parasite infectivity and capacity to multiply as the intracellular amastigote form [lo].…”

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Identification and Biosynthesis of N¹,N⁹‐Bis(Glutathionyl)Aminopropylcadaverine (Homotrypanothione) in Trypanosoma Cruzi

Hunter

Quesne

Fairlamb

1994

European Journal of Biochemistry

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Radiolabelling studies using tritiated ornithine, arginine and lysine, together with the relevant amino acid decarboxylase enzyme assays, indicate that the epimastigote stage of Trypanosoma cruzi is unable to synthesise significant amounts of putrescine and cadaverine de novo, compared to the amounts of these diamines scavenged from the growth medium. Radiolabelled putrescine is readily incorporated into spermidine, spennine and the trypanosomatid-specific polyamine-glutathione conjugate trypanothione (W,iP-bis(g1utathionyl)spermidine). Likewise, radiolabelled cadaverine is incorporated into the analogous polyamines aminopropylcadaverine, bis(aminopropy1)cadaverine and another major unidentified component. Subsequent studies showed this major component to be a novel polyamine-thiol conjugate whose structure was confirmed by chemical synthesis to be hr , N9-bis(glutathiony1)aminopropylcadaverine (homotrypanothione). Kinetic analyses using recombinant 7: cruzi trypanothione reductase demonstrated that homotrypanothione disulphide is readily reduced by this enzyme with kinetic parameters similar to trypanothione disulphide, suggesting that it is a physiological substrate in vivo. Thus the epimastigote form of 7: cruzi differs significantly from the African trypanosomes and Leishmania in (a) being unable to synthesise significant amounts of diamines de novo, (b) converting significant amounts of putrescine and cadaverine to spermine and bis(aminopropyl)cadaverine, respectively and (c) the ability to synthesise homotrypanothione as well as trypanothione. The implications of these findings with respect to the prospective chemotherapy of Chagas' disease are discussed.

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Identification and Biosynthesis of N¹,N⁹‐Bis(Glutathionyl)Aminopropylcadaverine (Homotrypanothione) in Trypanosoma Cruzi

Hunter

Quesne

Fairlamb

1994

European Journal of Biochemistry

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“…In the second strain it is blocked between ornithine and arginine, since the bacteria cannot grow with ornithine. The polyamines are known to be synthesized through two different pathways, one starting from arginine and the other from ornithine (13). Thus, the first mutant could not form polyamines during arginine starvation, whereas the second should be able to make them.…”

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“…Since arginine is a precursor of both putrescine and spermidine (13), starvation of arginine should have direct effects on polyvanine contents. To avoid these specific effects, E. coli JG151-1, his-was also studied for the polyamine efrect.…”

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A Requirement of Polyamines for Bacterial Division*

Inouye

Pardee

1970

Annals of the New York Academy of Sciences

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Synchronous cell division in an arginine auxotroph and a histidine auxotroph of Escherichia coli was obtained after starving for the required amino acid for 1 hr. However, cell division was not synchronized after starvation for 1 hr in another arginine auxotroph. This difference is proposed to depend on differences in the concentrations of polyamines in the cells. During amino acid starvation the ratio of putrescine concentration to spermidine concentration decreased in all strains, but it recovered afterward more rapidly in the third strain than in the other two. The cells divided when the ratio returned to normal in the Arg-mutants. Added putrescine permitted some of the cells of the first two mutants to divide sooner after amino acid starvation and thus eliminated synchrony. Spermidine added alone had no effect, but, when it was added together with putrescine, it restored synchronous division. Synchrony was established in the third mutant by adding spermidine after arginine starvation. Thus, both the variations in polyamine content and the effects of added polyamines suggest that the polyamines are essential in permitting cell division. We suggest that the molar ratio of putrescine to spermidine can be a critical factor for cell division. This effect of polyamines seems to be specific for cell division. Amino acid starvation does not induce delays in subsequent mass increase or deoxyribonucleic acid synthesis. Possible mechanisms of polyamine action are discussed.Escherichia coli can be caused to divide synchronously after starving the cells for amino acids for several hours (11). While applying this technique, we noted that one argmine auxotroph divided synchronously but another did not. In this paper we show that the difference between the strains might depend on their polyamine contents after arginine starvation. A high concentration of putrescine relative to spermidine appears to be necessary for cell division. In all amino acid starvation experiments, M9 medium was used. M9 medium consists of 7 g of Na2HPO4, 3 g of KH2PO4, 0.5 g of NaCl, 1 g of NH4CI, 0.2 g of MgS04-7H20, and 1 liter of water supplemented with 4 mg of glucose per ml and 2 pg of vitamin B, per ml. When thymidine, L-arginine, and L-histidine were required, they were added at the concentrations of 4, 50, and 20 ug/ml, respectively.Isolation of arginine auxotrophs. Arginine auxotrophs were isolated from E. coli 15T-by N-methyl-N'-nitro-N-nitrosoguanidine (NG) treatment followed by photo-bromo-uracil selection (1,8). Cells at 2 X 109/ml from an overnight culture of E. coli 1ST-were suspended in 1 mg/ml of NG in 0.2 M sodiun acetate buffer (pH 5.0) for 30 min at 37 C. These cells were washed, and a small inoculum was grown overnight in Penassay broth and diluted 20-fold with M9 medium, supplemented with 2 pg thymine and 50 ug L-arginine per ml and incubated at 37 C for 2 hr. A 4-ml amount of the culture was then filtered (HA membrane filter; 0.45-pum pore size; Millipore Corp., Bedford, Mass.), and the cells were suspended in 20 ml of M9 mediu...

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“…In many strains of E. coli the biosynthetic ornithine decarboxylase provides the predominant route for putrescine biosynthesis (7). The biosynthetic arginine decarboxylase appears to play a complementary role in maintaining intracellular polyamine levels.…”

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Regulation of polyamine biosynthesis in Escherichia coli by basic proteins.

Heller¹,

Rostomily²,

Kyriakidis³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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REGULATORY PATTERNS IN PUTRESCINE BIOSYNTHESIS IN ESCHERICHIA COLI

Cited by 62 publications

References 22 publications

Identification and Biosynthesis of N¹,N⁹‐Bis(Glutathionyl)Aminopropylcadaverine (Homotrypanothione) in Trypanosoma Cruzi

Identification and Biosynthesis of N¹,N⁹‐Bis(Glutathionyl)Aminopropylcadaverine (Homotrypanothione) in Trypanosoma Cruzi

A Requirement of Polyamines for Bacterial Division*

Regulation of polyamine biosynthesis in Escherichia coli by basic proteins.

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REGULATORY PATTERNS IN PUTRESCINE BIOSYNTHESIS IN ESCHERICHIA COLI

Cited by 62 publications

References 22 publications

Identification and Biosynthesis of N1,N9‐Bis(Glutathionyl)Aminopropylcadaverine (Homotrypanothione) in Trypanosoma Cruzi

Identification and Biosynthesis of N1,N9‐Bis(Glutathionyl)Aminopropylcadaverine (Homotrypanothione) in Trypanosoma Cruzi

A Requirement of Polyamines for Bacterial Division*

Regulation of polyamine biosynthesis in Escherichia coli by basic proteins.

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Identification and Biosynthesis of N¹,N⁹‐Bis(Glutathionyl)Aminopropylcadaverine (Homotrypanothione) in Trypanosoma Cruzi

Identification and Biosynthesis of N¹,N⁹‐Bis(Glutathionyl)Aminopropylcadaverine (Homotrypanothione) in Trypanosoma Cruzi