Regulation of dihydrodipicolinate synthase and aspartate kinase in Bacillus subtilis

Vold, Barbara S.; Szulmajster, Jekisiel; Carbone, Arnaldo

doi:10.1128/jb.121.3.970-974.1975

Cited by 35 publications

(13 citation statements)

References 12 publications

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“…This mutation differs from previously described thiosine resistance mutations (7,14,15,18,19,26,29). The spontaneous origin and high frequency of isolation of thiosine-resistant mutants with the same properties as PSPO1 indicate that the multiple phenotypic manifestations of this mutant are due to a single mutation.…”

Section: Discussioncontrasting

confidence: 52%

“…Mutants of yeast resistant to thiosine and with altered lysine-specific transport have been described (13). In bacteria thiosine-resistant mutants have been found which exhibit altered growth medium-dependent levels of lysyl tRNA synthetase (17,18), the absence of the threoninecontrolled aspartokinase-homoserine dehydrogenase complex activity in extracts (19), derepression of aspartokinase III (29), feedback densensitization of the lysine biosynthetic pathway at either of the two normally feedbacksensitive enzymes (aspartokinase or dihydrodipicolinic acid synthetase) (7,15,26), and decreased lysine transport by both the lysine-specific system and the general basic amino acid transport system for lysine, arginine, and ornithine (LAO system) (14).…”

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confidence: 99%

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Escherichia coli regulatory mutation affecting lysine transport and lysine decarboxylase

Popkin¹,

Maas²

1980

J Bacteriol

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A spontaneous thiosine-resistant mutant of Escherichia coli was shown to have the following characteristics: lowered initial rate of lysine uptake and lowered plateau level of accumulation of exogenous lysine by both the lysine-specific and the general basic amino acid transport systems; altered repressibility of these two lysine transport systems; a derepressed level of lysine decarboxylase; normal growth rate; parental levels of lysyl-transfer ribonucleic acid synthetase and the inducible and constitutive arginine and ornithine decarboxylases. Both the mutant (lysP) and its parent (lysP+) feed a lysine auxotroph when they are plated in proximity on solid medium. However, the feeding response was observable after 1 day less of incubation when the mutant was the feeding strain. Despite the derepressed level of lysine decarboxylase in exponential cultures of the mutant extracts of these cultures had no detectable cadaverine pool. Conjugation experiments established the following gene order: gyrA (formerly nalA) lysP metG his. All thiosine-resistant recombinants assayed showed reduced lysine transport. In many of these recombinants the derepression of lysine decarboxylase was not expressed.

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Section: Discussioncontrasting

confidence: 52%

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confidence: 99%

Escherichia coli regulatory mutation affecting lysine transport and lysine decarboxylase

Popkin¹,

Maas²

1980

J Bacteriol

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“…One of the lysine biosynthetic enzymes, dihydrodipicolinate synthase, was down‐regulated, but it is unlikely to be a key enzyme in lysine biosynthesis. Starvation or supplementation with lysine do not depress the expression and activity of dihydrodipicolinate synthase (Vold et al , 1975), which only increases significantly during sporulation in B. subtilis and B. cereus (Hoganson & Stahly, 1975; Vold et al , 1975).…”

Section: Resultsmentioning

confidence: 99%

Proteomic analysis of Bacillus cereus growing in liquid soil organic matter

Luo

Vilain

Voigt

et al. 2007

FEMS Microbiology Letters

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Bacillus cereus is believed to be a soil bacterium, but studied solely in laboratory culture media. The aim of this study was to assess the physiology of B. cereus growing on soil organic matter by a proteomic approach. Cells were cultured to mid-exponential phase in soil extracted solubilized organic matter (SESOM), which mimics the nutrient composition of soil, and in Luria-Bertani broth as control. Silver staining of the two-dimensional gels revealed 234 proteins spots up-regulated when cells were growing in SESOM, with 201 protein spots down-regulated. Forty-three of these differentially expressed proteins were detected by Colloidal Coomassie staining and identified by matrix assisted laser desorption ionization-time of flight MS of tryptic digests. These differentially expressed proteins covered a range of functions, primarily amino acid, lipid, carbohydrate and nucleic acid metabolism. These results suggested growth on soil-associated carbohydrates, fatty acids and/or amino acids, concomitant with shifts in cellular structure.

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“…The sensitivity of DHDPS to lysine differs widely. DHDPS from plants is strongly inhibited by lysine [ 34 ], while DHDPS from gram-negative bacteria such as E. coli [ 35 ] is less strongly inhibited by lysine, and most gram-positive bacteria, such as Bacillus subtilis [ 36 ] and Corynebacterium glutamicum [ 37 ], DHDPS is not inhibited by lysine at all. Therefore, FaDHDPS1 was similar to the DHDPS from most gram-positive bacteria.…”

Section: Discussionmentioning

confidence: 99%

Involvement of a dihydrodipicolinate synthase gene (FaDHDPS1) in fungal development, pathogenesis and stress responses in Fusarium asiaticum

et al. 2018

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BackgroundDihydrodipicolinate synthase (DHDPS) is an allosteric enzyme, which catalyzes the first unique step of lysine biosynthesis in prokaryotes, higher plants and some fungi. To date, the biological roles of DHDPS in filamentous fungi are poorly understood.ResultsIn this study, on the basis of comparative genome resequencing, a DHDPS gene was found to be specific in Fusarium asiaticum, named FaDHDPS1, which showed high amino acid identity to that of entomopathogenic fungus. Subcellular localization of the FaDHDPS1-GFP fusion protein was mainly concentrated in the cytoplasm of conidia and dispersed in the cytoplasm during conidial germination. To reveal the biological functions, both deletion and complementation mutants of FaDHDPS1 were generated. The results showed that the FaDHDPS1 deletion mutant was defective in conidiation, virulence and DON biosynthesis. In addition, deletion of FaDHDPS1 resulted in tolerance to sodium pyruvate, lysine, low temperature and Congo red.ConclusionResults of this study indicate that FaDHDPS1 plays an important role in the regulation of vegetative differentiation, pathogenesis and adaption to multiple stresses in F. asiaticum.Electronic supplementary materialThe online version of this article (10.1186/s12866-018-1268-7) contains supplementary material, which is available to authorized users.

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Regulation of dihydrodipicolinate synthase and aspartate kinase in Bacillus subtilis

Cited by 35 publications

References 12 publications

Escherichia coli regulatory mutation affecting lysine transport and lysine decarboxylase

Escherichia coli regulatory mutation affecting lysine transport and lysine decarboxylase

Proteomic analysis of Bacillus cereus growing in liquid soil organic matter

Involvement of a dihydrodipicolinate synthase gene (FaDHDPS1) in fungal development, pathogenesis and stress responses in Fusarium asiaticum

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