Formation of some extracellular enzymes during the exponential growth ofBacillus subtilis

Liebs, P.; Riedel, K.; Graba, J. P.; Schrapel, D.; Tischler, U.

doi:10.1007/bf02928073

Cited by 17 publications

(17 citation statements)

References 20 publications

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“…A similar hierarchy of amino acid utilization was observed for Bacillus subtilis cells growing in a medium containing ammonium casamino acids (Liebs et al, 1988). These authors observed that glutamate, aspartate, serine, and alanine were depleted from the growth medium at similar rates throughout the exponential growth.…”

Section: Discussionsupporting

confidence: 61%

The penicillin G acylase production by B. megaterium is amino acid consumption dependent

Pinotti

Souza

Giordano

et al. 2006

Biotech & Bioengineering

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Aiming at to enhance the production of penicillin G acylase (PGA) by Bacillus megaterium, we have performed flasks experiments using different medium composition. Using 51 g/L of casein hydrolyzed with Alcalase and 2.7 g/L of phenylacetic acid (PhAc), the following carbon substrates were tested, individually and combined: glucose, glycerol, and lactose (present in cheese whey). Glycerol and glucose showed to be effective nutrients for the microorganism growth but delayed the PGA production. Cheese whey always increased enzyme production and cell mass. However, lactose (present in cheese whey) was not a significant carbon source for B. megaterium. PhAc, amino acids, and small peptides present in the hydrolyzed casein were the actual carbon sources for enzyme production. Replacement of hydrolyzed casein by free amino acids, 10.0 g/L, led to a significant increase in enzyme production (app. 150%), with a preferential consumption of alanine, aspartic acid, glycine, serine, arginine, threonine, lysine, and glutamic acid. A decrease of the enzyme production was observed when 20.0 g/L of amino acids were used. Using the single omission technique, it was shown that none of the 18 tested amino acids was essential for enzyme production. The use of a medium containing eight of the preferentially consumed amino acids lead to similar enzyme production level obtained when using 18 amino acids. PhAc, up to 2.7 g/L, did not inhibit enzyme production, even if added at the beginning of the cultivation.

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Section: Discussionsupporting

confidence: 61%

The penicillin G acylase production by B. megaterium is amino acid consumption dependent

Pinotti

Souza

Giordano

et al. 2006

Biotech & Bioengineering

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“…B. subtilis additionally consumes arginine and asparagine, whereas E. coli only consumes asparagine under anaerobic conditions. These findings are in general agreement with previous reports that used more complex media (Liebs et al ., ; Pruss et al ., ; Selvarasu et al ., ) and confirm strong evolutionary conservation of the metabolic network.…”

Section: Discussionmentioning

confidence: 99%

Relation between chemotaxis and consumption of amino acids in bacteria

Yang

Pollard

Höfler

et al. 2015

Molecular Microbiology

140

132

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SummaryChemotaxis enables bacteria to navigate chemical gradients in their environment, accumulating toward high concentrations of attractants and avoiding high concentrations of repellents. Although finding nutrients is likely to be an important function of bacterial chemotaxis, not all characterized attractants are nutrients. Moreover, even for potential nutrients, the exact relation between the metabolic value of chemicals and their efficiency as chemoattractants has not been systematically explored. Here we compare the chemotactic response of amino acids with their use by bacteria for two well‐established models of chemotactic behavior, E scherichia coli and B acillus subtilis. We demonstrate that in E . coli chemotaxis toward amino acids indeed strongly correlates with their utilization. However, no such correlation is observed for B . subtilis, suggesting that in this case, the amino acids are not followed because of their nutritional value but rather as environmental cues.

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“…Poor expression of BcaP in amino acid-rich media may explain why ILV are utilized only in stationary phase, i.e., when CodY activity diminishes due to exhaustion of other amino acids and BcaP-mediated transport of ILV apparently resumes (52). Importantly, such a pattern of ILV utilization should extend the time when CodY is maintained in at least a partially active state.…”

Section: Discussionmentioning

confidence: 99%

Role of Branched-Chain Amino Acid Transport in Bacillus subtilis CodY Activity

Belitsky

2015

J Bacteriol

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CodY is a branched-chain amino acid-responsive transcriptional regulator that controls the expression of several dozen transcription units in Bacillus subtilis. The presence of isoleucine, valine, and leucine in the growth medium is essential for achieving high activity of CodY and for efficient regulation of the target genes. We identified three permeases-BcaP, BraB, and BrnQthat are responsible for the bulk of isoleucine and valine uptake and are also involved in leucine uptake. At least one more permease is capable of efficient leucine uptake, as well as low-affinity transport of isoleucine and valine. The lack of the first three permeases strongly reduced activity of CodY in an amino acid-containing growth medium. BcaP appears to be the most efficient isoleucine and valine permease responsible for their utilization as nitrogen sources. The previously described strong CodY-mediated repression of BcaP provides a mechanism for fine-tuning CodY activity by reducing the availability of amino acids and for delaying the utilization of isoleucine and valine as nitrogen and carbon sources under conditions of nutrient excess. IMPORTANCEBacillus subtilis CodY is a global transcriptional regulator that is activated by branched-chain amino acids (BCAA). Since the level of BCAA achieved by intracellular synthesis is insufficient to fully activate CodY, transport of BCAA from the environment is critical for CodY activation, but the permeases needed for such activation have not been previously identified. This study identifies three such permeases, reports their amino acid transport specificity, and reveals their impact on CodY activation. CodY is a global transcriptional regulator in Bacillus subtilis that controls, directly or indirectly, the expression of about 200 genes, most of them negatively (1-3). Many of the CodY-regulated genes are involved in nitrogen or carbon metabolism (1, 2, 4-7). CodY homologs are present in most low-GϩC Gram-positive bacteria and in many species have been shown to play a global role in metabolic regulation similar to that in B. subtilis, as well as in coordinating expression of virulence-associated functions with expression of metabolic genes (7, 8; see also, e.g., references 9 and 10 and references therein).B. subtilis CodY is a dimeric 259-residue protein that uses a winged helix-turn-helix motif to bind to DNA (11,12). The DNAbinding activity of CodY is increased by interaction with two types of effectors, branched-chain amino acids (BCAA; isoleucine [Ile], leucine [Leu], and valine [Val], collectively abbreviated as ILV) (13-17) and GTP (1,15,(18)(19)(20). The effect of GTP on CodY, however, may depend on simultaneous or prior interaction of CodY with ILV because mutant variants of CodY deficient in ILV binding lose most of the ability to regulate CodY-dependent genes (21, 22). The pools of ILV and GTP apparently reflect the nutritional status of the cells, allowing bacteria to change the pattern of CodY-dependent gene expression in response to availability of nutrients in the g...

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Formation of some extracellular enzymes during the exponential growth ofBacillus subtilis

Cited by 17 publications

References 20 publications

The penicillin G acylase production by B. megaterium is amino acid consumption dependent

The penicillin G acylase production by B. megaterium is amino acid consumption dependent

Relation between chemotaxis and consumption of amino acids in bacteria

Role of Branched-Chain Amino Acid Transport in Bacillus subtilis CodY Activity

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