prtR enhances the mRNA level of the Bacillus subtilis extracellular proteases

Takano, Teruo; Kawata, Mutsumi; Nagami, Yoichi; Uchiyama, Hiroo

doi:10.1128/jb.169.7.3044-3050.1987

Cited by 34 publications

(28 citation statements)

References 43 publications

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“…Several regulatory genes encoding small polypeptides of 46 to 65 amino acid residues which cause a higher level of expression of a class of extracellular proteins in B. subtilis have been reported, i.e., senS (45), degR (25,42,49), and degQ (3,48). The pleiotropic effects of these genes suggest that they are part of a global control mechanism affecting the synthesis of degradative enzymes.…”

Section: Discussionmentioning

confidence: 99%

“…Expression of degQ was shown to be controlled by DegS-DegU. This Production of a class of degradative enzymes in Bacillus subtilis, including an intracellular protease and several secreted enzymes (levansucrase, alkaline and metalloproteases, a-amylase, 3-glucanase[s], and xylanase) (3,5,11,29), is controlled at the transcriptional level by the DegSDegU two-component system and by at least two additional regulatory genes, degQ and degR, which encode small polypeptides of 46 and 60 amino acids, respectively (3,25,42,48,49).Although the two-component system is required for degradative enzyme production, the products of degQ and degR appear to be dispensable (48,49). Mutations were identified in both degS and degU leading to either deficiency of degradative enzyme production or a pleiotropic (Hy) phenotype, which includes hyperproduction of degradative enzymes, ability to sporulate in the presence of glucose, decreased genetic competence, and loss of flagella (6,12,17,23).…”

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“…Production of a class of degradative enzymes in Bacillus subtilis, including an intracellular protease and several secreted enzymes (levansucrase, alkaline and metalloproteases, a-amylase, 3-glucanase[s], and xylanase) (3,5,11,29), is controlled at the transcriptional level by the DegSDegU two-component system and by at least two additional regulatory genes, degQ and degR, which encode small polypeptides of 46 and 60 amino acids, respectively (3,25,42,48,49).…”

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DegS-DegU and ComP-ComA modulator-effector pairs control expression of the Bacillus subtilis pleiotropic regulatory gene degQ

et al. 1991

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Production of a class of both secreted and intracellular degradative enzymes in Bacillus subtilis is regulated at the transcriptional level by a signal transduction pathway which includes the DegS-DegU two-component system and at least two additional regulatory genes, degQ and degR, encoding polypeptides of 46 and 60 amino acids, respectively. Expression of degQ was shown to be controlled by DegS-DegU. This Production of a class of degradative enzymes in Bacillus subtilis, including an intracellular protease and several secreted enzymes (levansucrase, alkaline and metalloproteases, a-amylase, 3-glucanase[s], and xylanase) (3,5,11,29), is controlled at the transcriptional level by the DegSDegU two-component system and by at least two additional regulatory genes, degQ and degR, which encode small polypeptides of 46 and 60 amino acids, respectively (3,25,42,48,49).Although the two-component system is required for degradative enzyme production, the products of degQ and degR appear to be dispensable (48,49). Mutations were identified in both degS and degU leading to either deficiency of degradative enzyme production or a pleiotropic (Hy) phenotype, which includes hyperproduction of degradative enzymes, ability to sporulate in the presence of glucose, decreased genetic competence, and loss of flagella (6,12,17,23).Since degradative enzyme production requires both the DegS protein kinase and the DegU effector, we postulated that the phosphorylated form of DegU may be necessary for this process. On the other hand, we postulate that the nonphosphorylated form of DegU may be required for competence (23, 28; this report). This hypothesis is supported by the following observations: (i) the degUJ46 mutation abolishing the putative site of phosphorylation of the DegU effector did not abolish competence (23), and (ii) deletion of the degS gene did not strongly reduce competence (this report).The degQ36 mutation, a single base change at position -10 leading to overexpression of the degQ gene, gave a Hy phenotype similar to that of the degS(Hy) and degU(Hy) * Corresponding author. mutations (3, 48). The increase of degradative enzyme production due to overproduction of DegQ is, however, strictly dependent upon the presence of a functional DegSDegU two-component system (3; this report).We previously reported that expression of degQ was decreased in strains carrying either a deletion of degS and degU or a degU32(Hy) mutation (23). In this report, we show that degQ expression is regulated by a second twocomponent system controlling competence in B. subtilis: 47). Several findings had suggested that this could be the case: (i) DegS-DegU and ComP-ComA show strong amino acid sequence similarities, (ii) both of these two-component systems control the expression of competence, and (iii) the degQ, comP, and comA genes are located at adjacent positions on the B. subtilis chromosome (47).The DegS, DegU, and DegQ proteins are produced at different times during growth. The degS-degU operon is expressed throughout the exponential growth pha...

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DegS-DegU and ComP-ComA modulator-effector pairs control expression of the Bacillus subtilis pleiotropic regulatory gene degQ

et al. 1991

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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.…”

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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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“…With these mutants and the cloned genes available, the mechanism for the enhanced production of extracellular enzymes can be studied in detail. degR, senN, degQ, and sacU have been shown to exert their stimulatory effects at the transcriptional level (28,35,42). However, in the sacU minus mutant strain, no enhanced production of extracellular enzymes can be observed with cells carrying either degR or degQ on a multicopy plasmid (1,34).…”

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Cloning and characterization of a pair of novel genes that regulate production of extracellular enzymes in Bacillus subtilis

1991

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Two novel Bacillus subtilis genes that regulate the production of several extracellular enzymes were cloned and characterized. These two genes are organized as part of an operon. When cloned in a multicopy plasmid, the first gene (tenA, transcription enhancement) stimulates alkaline protease production at the transcriptional level. The second gene (tenI) exerts an opposite effect to reduce alkaline protease production. The production of neutral protease, levansucrase, and alkaline protease can be stimulated up to 11-to Bacillus subtilis is capable of secreting a wide variety of extracellular enzymes (proteases, a-amylase, levansucrase, and P-glucanases) directly into the medium (22). Several mutants that can stimulate the production of extracellular enzymes have been isolated. These mutants carry mutations in degQ and sacU (12,14). Structural genes encoding degQ and sacU have been cloned (1,8,11,34,36,45). Furthermore, the cloning of several regulatory genes from B. subtilis, B. natto, and B. stearothermophilus has been shown to enhance the production of extracellular enzymes when these genes are in a multicopy plasmid. These genes are sacV (17), degR (19, 47), senS (38), senN (39,42), and degT (33). The size of the protein products derived from these genes varies from small polypeptides (46 to 65 amino acids for the degR, sacV, senS, and senN products) to larger polypeptides (372 amino acids for the degT product). Although these gene products show no sequence homology with each other, they all stimulate the production of extracellular enzymes. The target genes encoding extracellular enzymes such as aprE (alkaline protease) (30, 41), nprE (neutral protease) (46), amyE (oa-amylase) (44), and sacB (levansucrase) (32) have also been cloned. With these mutants and the cloned genes available, the mechanism for the enhanced production of extracellular enzymes can be studied in detail. degR, senN, degQ, and sacU have been shown to exert their stimulatory effects at the transcriptional level (28,35,42). However, in the sacU minus mutant strain, no enhanced production of extracellular enzymes can be observed with cells carrying either degR or degQ on a multicopy plasmid (1,34).In this report, we describe in detail the cloning, nucleotide sequence, genetic mapping, and organization of a set of two novel genes from B. subtilis that can regulate the production of several extracellular enzymes. They were isolated by using a shotgun cloning approach and were selected by their abilities to stimulate the production of alkaline protease. The * Corresponding author. characterization of these genes and their roles in regulating gene expression are discussed. MATERIALS AND METHODSPlasmids. Plasmid pUB18 (42), a derivative of pUB110, was used for routine subcloning in B. subtilis. pPQ is a pUB18 derivative carrying degQ (40). Bluescribe plasmid from Escherichia coli was used for cloning and doublestranded DNA sequencing. Standard DNA transformation was performed by the competent cell method in B. subtilis (29) and E. coli (16).Med...

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prtR enhances the mRNA level of the Bacillus subtilis extracellular proteases

Cited by 34 publications

References 43 publications

DegS-DegU and ComP-ComA modulator-effector pairs control expression of the Bacillus subtilis pleiotropic regulatory gene degQ

DegS-DegU and ComP-ComA modulator-effector pairs control expression of the Bacillus subtilis pleiotropic regulatory gene degQ

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

Cloning and characterization of a pair of novel genes that regulate production of extracellular enzymes in Bacillus subtilis

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