Effects of diphenylamine on carotenoids and menaquinones in bacterial membranes

Saltón, M. R. J.; Schmitt, Margreth D.

doi:10.1016/0005-2736(67)90114-9

Cited by 41 publications

(22 citation statements)

References 19 publications

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“…However, two alternatives are possible: (i) M . roseus has an efficient repair mechanism which renders it resistant to photodynamic killing unless an exogenous photosensitizer is present, (ii) DPA, which can be incorporated into bacterial membranes (15), may interfere with synthesis or function of endogenous photosensitizers. In tests for endogenous photosensitization, cells grown in the presence of DPA released more cations and more UV-absorbing material than noninhibited cells suggesting that DPA or carotenoid deficiency altered membrane permeability.…”

Section: Resultsmentioning

confidence: 99%

Action of light on Micrococcus roseus

Schwartzel¹,

Cooney²

1974

Can. J. Microbiol.

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1974. Action of light on Micrococc~ts roseus. Can. J.Microbiol. 20: 1015-1021. Micrococc~ts roseus is killed by exposure to a continuous spectrum of white light (3000 ft-c (32 292 Im/m2)) in the presence of air and the dye, toluidine blue. Comparison of rates of photodynamic killing for log and stationary phase cells and for two pigmentation mutants indicated that photosensitivity could not be correlated with amount of carotenoid or with carotenoid-chromophore length. Moreover, cells grown in medium containing diphenylamine (DPA) did not contain significant quantities of colored carotenoids; they were not as sensitive to photodynamic killing as fully pigmented cclls. Photodynamic killing was accompanied by selective release of magnesium and calcium and by release of UV-absorbing material. In the absence of added photosensitizer, M. rosetts, the two mutants, or DPA-inhibited cells were not killed when exposed to white light at intensities as high as 22 000 ft-c (236 806 Im/m2) for a s long as 9 h, and cells did not release UV-absorbing material. Under these conditions M . roseus and the yellow mutant did not release as much magnesium or calcium as when subjected to photodynamic killing, but DPA-grown cells leaked sodium, magnesium, and calcium. These observations are consistent with several suggestions: (i) carotenoids do not serve as photochemical buffers in M. roserts; (ii) growth in medium containing DPA or mutations leading to altered pigmentation change membrane organization leading to altered photosensitivity; (iii) M. roseus has an efficient repair mechanism which renders it resistant to photodynamic killing unless an exogenous photosensitizer is present. SCHWARTZEL, E. H., et J. J. COONEY. 1974. Action of light on Micrococcus roseus. Can. J.Microbiol. 20: 1015-1021. Micrococcus roselts est tuC par I'exposition un spectre continu de lumiere blanche (3000 ft-c (32 292 Im/m2)) en presence de I'air et d'un colorant toluidine bleu. La comparaison des taux de mortalite photodynamique pour les cellules en phase logarithmique et en phase stationnaire et pour les deux mutants a la pigmentation indique que la photosensibilite ne peut pas &tre corrdee avec la quantitt de carotkno'ide ou avec la longueur du chromophore caroteno'ide. En plus, les cellules qui se sont developpees dans un milieu contenant la diphenylamine (DPA) ne contiennent pas de quantitt significative de carotenoi'des colorees; elles ne sont pas aussi sensibles a la mortalit6 photodynamique que les cellules entierement pigmentees. La mortalit6 photodynamique est accompagnke par une liberation selective du magntsium et du calcium e t de materiel absorbant I'UV. En I'absence de photosensibilisateurs, M . roseus, les deux mutants, ou lcs cellules inhibks au DPA, ne sont pas tuees lorsqu'elles sont exposees a la lumitre blanche a des intensites aussi hautes que 22 000 ft-c (236 806 Im/m2) pour aussi longtemps que 9 1.1, et les cellules ne liberent pas de materiel absorbant I'UV. Sous ces conditions, M . rosetts et le mutant jaune ne liberent pas autant d...

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Section: Resultsmentioning

confidence: 99%

Action of light on Micrococcus roseus

Schwartzel¹,

Cooney²

1974

Can. J. Microbiol.

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“…The localization of other "lipid-soluble" components of the bacterial cell, including carotenoids and menaquinones, has been reported in a number of studies (Matthews and Sistrom, 1959;Salton and Ehtisham-ud-din, 1965;Bishop and King, 1962;Salton and Schmitt, 1967a). The carotenoid pigments have been particularly useful "lipid markers" in studies of membrane isolation, fractionation, and characterization (Salton, 1967b).…”

Section: B Lipids and Lipid-soluble Componentsmentioning

confidence: 93%

The Bacterial Membrane

Saltón

1971

Biomembranes

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“…Strains RB1, RB1120, RB1250, and RB1255 were grown in LB medium with and without the iron chelator ␣,␣-dipyridyl. The bacterial membranes were extracted with chloroform-methanol (17), spotted onto a thin-layer plate, and developed with iso-octane-diethyl ether (31). Menadione, which lacks an isoprenoid side group, and menatetrenone (MK4), which has four isoprenoid units in the side chain compared with seven isoprenoid units in MK7 (the isoprenolog formed by B. subtilis), were included as controls.…”

Section: Resultsmentioning

confidence: 99%

“…Membranes were extracted in chloroform-methanol (2:1, vol/vol) and prepared by following the procedure of Meganathan and Cofell (17). Thin-layer chromatography was performed by following the procedure of Salton and Schmitt (31). A silica gel thin-layer plate (type SI250; Baker) was preactivated at 100ЊC for 30 min.…”

Section: Methodsmentioning

confidence: 99%

Duplicate isochorismate synthase genes of Bacillus subtilis: regulation and involvement in the biosyntheses of menaquinone and 2,3-dihydroxybenzoate

Rowland

Taber

1996

J Bacteriol

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Bacillus subtilis has duplicate isochorismate synthase genes, menF and dhbC. Isochorismate synthase is involved in the biosynthesis of both the respiratory chain component menaquinone (MK) and the siderophore 2,3-dihydroxybenzoate (DHB). Several menF and dhbC deletion mutants were constructed to identify the contribution made by each gene product to MK and DHB biosynthesis. menF deletion mutants were able to produce wild-type levels of MK and DHB, suggesting that the dhbC gene product is able to compensate for the lack of MenF. However, a dhbC deletion mutant produced wild-type levels of MK but was DHB deficient, indicating that MenF is unable to compensate for the lack of DhbC. A menF dhbC double-deletion mutant was both MK and DHB deficient. Transcription analysis showed that expression of dhbC, but not of menF, is regulated by iron concentration. A dhbA::lacZ fusion strain was constructed to examine the effects of mutations to the iron box sequence within the dhb promoter region. These mutations abolished the iron-regulated transcription of the dhb genes, suggesting that a Fur-like repressor protein exists in B. subtilis.Isochorismate synthase is responsible for converting chorismate to isochorismate and is necessary for the biosynthesis of both the respiratory chain component menaquinone (MK) and the Bacillus subtilis siderophore 2,3-dihydroxybenzoate (DHB) (Fig. 1). Although it is known that the carbon source, growth phase, and oxygen tension have regulatory effects, the actual signals that induce expression of respiratory chain components are unknown (37). However, the production of DHB is known to be regulated by iron concentration (1,25,26). Therefore, isochorismate is required by cells under very different environmental conditions.B. subtilis has two distinct isochorismate synthases encoded by the menF (30) and dhbC (29) genes. MenF and DhbC are 47% identical at the DNA level and have 35% amino acid identity (29). menF is a promoter-proximal gene of the MK biosynthetic gene cluster located at 273Њ on the chromosome (30,38). MK is a lipophilic, nonprotein redox component mediating electron transfer between dehydrogenases and cytochromes (37). dhbC is the second gene of the DHB biosynthetic gene cluster located at 291Њ on the chromosome (29). Under conditions of iron deprivation, B. subtilis synthesizes DHB, a component of the specific transport system for the uptake of extracellular iron (1,25,26). This is not the only instance of gene duplication in B. subtilis. There are two thymidylate synthetases, TSaseA and TSaseB, that are encoded by the unlinked thyA and thyB genes, respectively (22). Both enzymes are functional in bacteria grown at 37ЊC or lower temperatures, but only TSaseA is active at 46ЊC (22). There are two different a-type terminal oxidases in B. subtilis that are encoded by separate loci (32). One of the oxidases is associated with a heme C-containing unit (32). The two membrane alkaline phosphatases of B. subtilis have substantial differences with respect to molecular weight, substrate sp...

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Effects of diphenylamine on carotenoids and menaquinones in bacterial membranes

Cited by 41 publications

References 19 publications

Action of light on Micrococcus roseus

Action of light on Micrococcus roseus

The Bacterial Membrane

Duplicate isochorismate synthase genes of Bacillus subtilis: regulation and involvement in the biosyntheses of menaquinone and 2,3-dihydroxybenzoate

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