A novel Bacillus subtilis gene involved in negative control of sporulation and degradative-enzyme production

Honjo, Masaru; Nakayama, Akira; Fukazawa, Kazuki; Kawamura, K.; Ando, Kazunori; Hori, Michiyo; Furutani, Yoshio

doi:10.1128/jb.172.4.1783-1790.1990

Cited by 56 publications

(40 citation statements)

References 41 publications

(27 reference statements)

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“…It involves protection of a relatively large region in the DNase I footprint (50 to 120 bp), and the protein appears to recognize some kind of structure in the DNA. A B. subtilis switch protein, 14 kDa, that alters the specificity of RNA polymerase containing cK. iS involved during the transition from morphological stages IV to V of sporulation (15).…”

Section: Resultsmentioning

confidence: 99%

“…Like spoO genes that are also required for initiation of sporulation, aprE expression is controlled by several regulatory genes, such as degU (11), degQ (1,31), degR (28,32), hpr (12,21), sen (30), abrB (6), pai (14), and sin (8). Henner et al (11) have identified target sites of hpr, degQ, and degU regulatory genes in the aprE gene by using several B. subtilis strains that have a series of promoter upstream deletions in aprE.…”

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confidence: 99%

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The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein

Gaur¹,

Oppenheim²,

Smith³

1991

J Bacteriol

108

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The sin gene of Bacillus subtilis encodes a dual-function regulatory protein, Sin, which is a negative as well as a positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Sin has been purified to homogeneity by using a simple two-step procedure. It was found to bind to the developmentally regulated aprE (alkaline protease) gene at two sites in vitro. The stronger Sin-binding site (SBS-1) is located more than 200 bp upstream from the transcription start site. It is required for Sin repression of aprE expression in vivo, as strains bearing SBS-1 deletions were not affected by the sin gene. The second, weaker Sin-binding site lies on a DNA fragment that contains the aprE promoter. Results of DNase I, exonuclease III, and dimethyl sulfate footprinting analysis of SBS-1 suggested that Sin binding involves two adjacent binding sites which appear to contain two different partial dyad symmetries. An analysis of the predicted amino acid sequence of Sin revealed a potential leucine zipper protein dimerization motif which is flanked by two helix-turn-helix motifs that could be involved in recognizing two different dyad symmetries.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein

Gaur¹,

Oppenheim²,

Smith³

1991

J Bacteriol

108

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“…Multiple copies of the degR (30,42,50), degQ (2,49), senS (46), and tenA (33) genes result in the overproduction of the extracellular proteases. On the other hand, the abrB (10), hpr (35), sin (12), and pai (16) loci are involved in negative regulation, and overproduction of the products of these genes inhibits the production of the exoproteases. In this complex regulatory network of exoprotease production, the two-component regulatory system, degS-degU, plays a central role (6,28).…”

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confidence: 99%

Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis

et al. 1994

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Bacillus subtilis secretes extracellular proteases whose production is positively regulated by a two-component regulatory system, DegS-DegU, and other regulatory factors including DegR. To identify an additional regulatory gene(s) for exoprotease production, we performed a shotgun cloning in the cell carrying multiple copies of degR and found a transformant producing large amounts of the exoproteases. The plasmid in this transformant, pLC1, showed a synergistic effect with multiple copies of degR on the production of the extracellular proteases, and it required degS for its enhancing effect. The DNA region responsible for the enhancement contained the proB gene, as shown by restriction analyses and sequence determination. The proB gene encoding Sy-glutamyl kinase was followed by the proA gene encoding glutamyl--y-semialdehyde dehydrogenase at an interval of 39 nucleotides, suggesting that the genes constitute an operon. pLC1 contained the complete proB gene and a part ofproA lacking the proA C-terminal region. It was also found that proB on the chromosome showed a synergistic effect with multiple copies of degR. We consider on the basis of these results that the metabolic intermediate, y-glutamyl phosphate, would transmit a signal to DegS, resulting in a higher level of phosphorylated DegU. Possible involvement of DegR in this process is discussed.

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“…To determine whether histidase expression can be activated by depletion of guanosine nucleotide pools, decoyinine, an inhibitor of GMP synthetase (15), was added to exponentially growing cultures of strains 168 and SF168R (hutR4). Decoyinine treatment caused no alteration in histidase expression in wild-type cultures grown in glucose minimal medium containing either glutamate-NH4Cl-histidine or histidine and a mixture of 16 amino acids as nitrogen sources (data not shown). However, histidase levels increased 40-fold after the addition of decoyinine to a HutR mutant culture growing exponentially in glucose minimal medium containing histidine and a mixture of 16 amino acids (Fig.…”

Section: Methodsmentioning

confidence: 99%

“…To determine whether any of the gene products known to alter gene expression during stationary growth phase also regulate hut expression, histidase expression was examined in strains containing mutations in the comA (9), comP (9), degUS (30), sin (28,32), pai (16), hpr (32), sigH (28), spoOA (28), spoOB (28) the autoradiogram showed that the relative levels of hutP RNA were 1 in T0.85 cells (Fig. 2, lane 1 Regulation ofhut expression by catabolite repression during stationary growth phase.…”

Section: Methodsmentioning

confidence: 99%

Activation of the Bacillus subtilis hut operon at the onset of stationary growth phase in nutrient sporulation medium results primarily from the relief of amino acid repression of histidine transport

1993

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During growth of Bacillus subtilis in nutrient sporulation medium containing histidine (DSM-His medium), the expression of histidase, the first enzyme in the histidine-degradative pathway (hut), is derepressed 40-to 200- When Bacillus subtilis cultures enter stationary growth phase in nutrient sporulation medium, the expression of gene products which allow the bacteria to adapt to their altered growth conditions is derepressed. Cells become motile, secrete a number of degradative enzymes, synthesize antibiotics, and, ultimately, can initiate the process of sporulation (28,30,32). All of these processes help the cells to survive under environmental conditions which are not optimal for growth.We have been studying the regulation of the enzymes responsible for histidine utilization (hut) in B. subtilis. The genes encoding the four enzymes that catalyze histidine degradation are organized as a multicistronic operon in B. subtilis (5,17,26). The first open reading frame in the hut operon, hutP, encodes a regulatory protein, which activates hut expression in trans (10,26). Downstream of the hutP gene is the hutH gene, which encodes histidase, the first enzyme in histidine degradation (26). A nucleotide sequence which could form a stem-loop structure lies between the hutP and hutH genes. Antitermination of hut transcription at this putative stem-loop structure has been proposed to mediate histidine-dependent induction of hut expression (26).Expression of the hut operon is highly regulated in response to nutrient availability in B. subtilis. hut expression is induced by histidine and repressed by rapidly metabolizable carbon compounds such as glucose, glycerol, or malate (5). Growth in the presence of a mixture of amino acids strongly inhibits synthesis of the hut enzymes (2). Mutations which alter regulation of the hut operon have been isolated. The * Corresponding author. hutC1 mutation allows expression of the hut enzymes in the absence of the inducer, histidine (5). hut expression is insensitive to regulation by catabolite repression in strains containing the hutR4 mutation (2, 11). Both the hutCl and hutR4 mutations are tightly linked to the hutH locus by transformation (5, 11).In this article, we report that hut expression is repressed during exponential growth in nutrient sporulation medium, but its expression completely derepresses at the onset of stationary growth phase. The postexponential activation of hut expression in this medium was investigated to identify factors regulating gene expression during this period of environmental stress. Derepression of hut expression during stationary growth in nutrient sporulation medium appears to be mediated primarily by the relief of amino acid repression of histidine transport. MATERIALS AND METHODS

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A novel Bacillus subtilis gene involved in negative control of sporulation and degradative-enzyme production

Cited by 56 publications

References 41 publications

The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein

The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein

Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis

Activation of the Bacillus subtilis hut operon at the onset of stationary growth phase in nutrient sporulation medium results primarily from the relief of amino acid repression of histidine transport

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