Transcriptional regulation of a <i>Bacillus subtilis</i> dipeptide transport operon

Slack, Frank J.; Mueller, Judith; Strauch, Mark A.; Mathiopoulos, C.; Sonenshein, Abraham L.

doi:10.1111/j.1365-2958.1991.tb00815.x

Cited by 75 publications

(79 citation statements)

References 40 publications

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“…The spoVG-lacZ and spoIIG-lacZ fusions were introduced into strains SMY and MB170 by transduction, by using SPI lysates of strains ZB308 and EU8743, respectively (12,46). The spoIIA-lacZ fusion was introduced by integration of plasmid pPP81 (27) (35) into the unique EcoRI site of pDG581 (3; see Fig. 4).…”

Section: Methodsmentioning

confidence: 99%

“…Phosphorylated SpoOA seems to have two activities that control stationary-phase events. It acts as a repressor of the abrB gene (41), whose product is itself a repressor of many genes expressed in the stationary phase (28,35,42,46). SpoOA also acts as a direct transcriptional activator of some essential sporulation genes, including spoILA (4,25) and spoIIG (32, 32a).…”

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confidence: 99%

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Role of the Bacillus subtilis gsiA gene in regulation of early sporulation gene expression

Mueller

Sonenshein

1992

J Bacteriol

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The BaciUlus subtilis gsiA operon was induced rapidly, but transiently, as cells entered the stationary phase in nutrient broth medium. A mutation at the gsiC locus caused sporulation to be defective and expression of gsi4 to be elevated and prolonged. The sporulation defect in this strain was apparently due to persistent expression of gsiA, since a gsiA null mutation restored sporulation to wild-type levels. Detailed mapping experiments revealed that the gsiC82 mutation lies within the kinA gene, which encodes the histidine protein kinase member of a two-component regulatory system. Since mutations in this gene caused a substantial blockage in expression ofspoIL4, spoIIG, and spoIID genes, it seems that accumulation of a product of the gsiAl operon interferes with sporulation by blocking the completion of stage II. It apparently does so by inhibiting or counteracting the activity of KinA.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

Role of the Bacillus subtilis gsiA gene in regulation of early sporulation gene expression

Mueller

Sonenshein

1992

J Bacteriol

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“…SpoOA is a DNA-binding protein whose capacity to turn on or turn off transcription of early-stationary-phase and sporulation genes is governed at the level of its phosphorylation by protein kinases (3). Activated SpoOA protein reduces the steady-state level of AbrB (13,39), a negative regulator of many stationary-phase-induced genes (38), including the dci4 operon (34). However, expression of dciA in growing cells is repressed even in abrB mutant strains (34), suggesting that AbrB is not the only factor that prevents dciA transcription in exponential-phase cells.…”

mentioning

confidence: 99%

“…This operon is transcribed at a very low level in vegetative cells in a medium that contains rapidly metabolizable sources of carbon, nitrogen, and phosphorus and is induced rapidly by all conditions that initiate sporulation (21,34). Stationary-phase induction of the dciA operon is known to be controlled indirectly by the product of the spoOA gene (34). SpoOA is a DNA-binding protein whose capacity to turn on or turn off transcription of early-stationary-phase and sporulation genes is governed at the level of its phosphorylation by protein kinases (3).…”

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confidence: 99%

Mutations that relieve nutritional repression of the Bacillus subtilis dipeptide permease operon

1993

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The Bacillus subtilis dcU operon encodes a dipeptide transport complex that is induced rapidly as cells enter stationary phase and initiate sporulation. Expression of this operon in growing cells is repressed by glucose, by a mixture of amino acids, and by the AbrB protein. A genetic screen was devised to identify mutations that allow inappropriate expression from the dcL4 promoter during growth. These mutations resulted in increased dci4 transcription during growth in nutrient broth, in minimal amino acids medium, and in minimal glucose medium. Some of the mutations, called des (dci control site), were cloned and shown by sequence analysis to cluster near the start site of dci4 transcription. Primer extension and in vitro transcription analysis revealed that the dcs mutations did not create a new promoter. These mutations may therefore disrupt an operator site necessary for the binding of a negative regulator responsive to the nutritional state of the cell. The dcs mutant promoters were still subject to AbrB control, suggesting that the dci4 operon is regulated by at least two proteins, AbrB and a nutritionally responsive regulator. The gene(s) for the putative nutritional regulator may be defined by the cod (control ofdciA) mutations, which appeared to relieve amino acid and glucose repression ofdci4 by altering a diffusible factor. An abrB cod double mutant exhibited high-level expression ofdci4 during exponential growth phase.In response to conditions of carbon, nitrogen, or phosphorus limitation, Bacillus subtilis cells undergo a primitive metamorphosis to produce an environmentally resistant spore (19), but the mechanism by which initiation of sporulation is triggered by nutrient depletion is poorly understood (37). The expression of many genes induced as the cells enter stationary phase is known to be regulated by carbon and nitrogen sources (9) and to require the action of various signal transduction systems and transcriptional regulators (for reviews, see references 15 and 36). The relationship between these regulators and the nutritional response is obscure, however. Some genes subject to such regulation, such as spoVG (12), are required for sporulation, but others, such as aprE (8), amyE (25), and gsiA (23), are not. The hut (histidine utilization) operon (1, 26) and the citB gene (5, 10), which encodes aconitase, are also induced early in stationary phase and are repressed independently by a mixture of amino acids and by rapidly metabolizable carbon sources. However, the molecular mechanisms of glucose repression and amino acid repression in B. subtilis remain elusive. Our studies have focused on the regulation of the dci4 (decoyinine induced [21]) operon as a model system for understanding nutritional control phenomena that occur at the onset of Bacillus development.In previous work, we showed that the dci4 operon encodes a dipeptide transport system that is dispensable for sporulation but may assist the cells in adapting to poor nutrient conditions (20). This operon is transcribed at a very low lev...

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“…b dppA was the dipeptide transport protein of Bacillus methanolicus [9], while dciAA was the gene product of the regulator of the dipeptide transport operon (dciAA) [26] of B. subtilis. The highly homologous regions are shaded.…”

Section: Purification Of D-methionine Amidase and Determination Of Nhmentioning

confidence: 99%

New thermostable d-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for d-phenylalanine production

Baek

Song

Lee

et al. 2003

Enzyme and Microbial Technology

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A new thermostable d-methionine amidase was found in a cell-free extract of Brevibacillus borstelensis BCS-1. After five steps of purification, the specific activity increased approximately 207-fold and the purity was more than 98%. The molecular weight of the enzyme was estimated to be 199 kDa by gel permeation chromatography and 30 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which indicates that the thermostable d-methionine amidase was a homo-hexamer consisting of a single subunit. The purified enzyme was stable up to 65 • C within a broad pH range from 6.5 to 10.0, and its maximum activity was measured at pH 9.5 and 70 • C. The enzyme activity increased about five-fold with the addition of Co 2+ , yet was strongly inhibited by Hg 2+ , 2-mercaptoethanol, dithiothreitol, and ethylenediaminetetracetic acid.The thermostable d-methionine amidase exhibited a high amidase activity and d-stereospecificity toward d-amino acid amides and esters, yet did not hydrolyze d-peptides. The catalytic efficiencies (k cat /K m , mM −1 s −1 ) of the enzyme for d-methioninamide and d-alaninamide were 3086 and 21.5, respectively, and the enantiomeric excess (ee) and enantiomeric ratio of d-phenylalanine produced from dl-phenylalaninamide were 97.1 and 196%, respectively.

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Transcriptional regulation of a Bacillus subtilis dipeptide transport operon

Cited by 75 publications

References 40 publications

Role of the Bacillus subtilis gsiA gene in regulation of early sporulation gene expression

Role of the Bacillus subtilis gsiA gene in regulation of early sporulation gene expression

Mutations that relieve nutritional repression of the Bacillus subtilis dipeptide permease operon

New thermostable d-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for d-phenylalanine production

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