Regulation of xylanolytic enzymes in Bacillus subtilis

Lindner, Cordula; Stülke, Jörg; Hecker, Michael

doi:10.1099/00221287-140-4-753

Cited by 73 publications

(54 citation statements)

References 24 publications

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“…This induction of the ion gene was significant, because the level of xynA mRNA did not change in response to any of the conditions analyzed in this study (data not shown). xynA codes for the enzyme xylanase of B. subtilis (40). In a sigB mutant of B. subtilis, the ion gene was induced at the same rate, indicating that the induction of the B. subtilis ion gene may be independent of aB.…”

Section: G C T G ã P C I S a T C T A A A G T C A C A G T C A C A T G mentioning

confidence: 97%

Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene

et al. 1994

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The kon gene of Escherichia coli encodes the ATP-dependent serine protease La and belongs to the family of c32-dependent heat shock genes. In this paper, we report the cloning and characterization of the Ion gene from the gram-positive bacterium Bacillus subtilis. The nucleotide sequence of the Ion locus, which is localized upstream of the heDL4XCDBL operon, was determined. The Ion gene codes for an 87-kDa protein consisting of 774 amino acid residues. A comparison of the deduced amino acid sequence with previously described ion gene products from E. coli, Bacillus brevis, and Myxococcus xanthus revealed strong homologies among all known bacterial Lon proteins. Like the E. coli ion gene, the B. subtilis Ion gene is induced by heat shock. Furthermore, the amount of Ion-specific mRNA is increased after salt, ethanol, and oxidative stress as well as after treatment with puromycin. The potential promoter region does not show similarities to promoters recognized by o+32 of E. coli but contains sequences which resemble promoters recognized by the vegetative RNA polymerase EoA of B. subtilis. A second gene designated orJX is suggested to be transcribed together with ion and encodes a protein with 195 amino acid residues and a calculated molecular weight of 22,000.ATP-dependent proteases are involved in the regulation of the level of a number of proteins with short half-lives, such as SulA and RcsA of Escherichia coli (25,26). In addition to biologically active proteins, many damaged and abnormal proteins resulting from misfolding, premature termination, or denaturation are subjected to ATP-dependent proteolytic degradation. During various stresses, increasing amounts of misfolded and damaged proteins may accumulate. Hence, the ATP-dependent proteases are also important during stress. In E. coli, two forms of energy-dependent proteolytic systems, the Lon (La) (11,14) and Clp (32,36) proteases, have been fairly well characterized. Lon (12,22,46) and ClpP (37) belong to the family of heat shock proteins. The ATP-dependent serine protease La is encoded by the ion gene of E. coli. Mutations in ion result in a pleiotropic phenotype of E. coli cells, with an increased sensitivity to UV light, mucoidy, filamentous growth, and defects in the lysogenicity of some bacteriophages and in the degradation of regulatory or abnormal proteins (26).Although extracellular proteases have been a matter of extensive investigation in various bacilli because of their industrial application, the knowledge of the structure and function of ATP-dependent proteases in Bacillus species is still very limited. stresses. According to their regulation, the heat shock proteins of B. subtifis can be arranged into at least two groups (29). Gene products of the groESL and the dnaK operons represent members of the first group. The heat induction of these proteins requires the vegetative sigma factor orA of B. subtifis (9) and a conserved palindromic structure (CIRCE) just downstream of the start point of transcription (50,67,70). The alternative sigma factor...

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Section: G C T G ã P C I S a T C T A A A G T C A C A G T C A C A T G mentioning

confidence: 97%

Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene

et al. 1994

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“…One unit of ␤-galactosidase activity is defined as the amount of enzyme which produces 1 nmol of o-nitrophenol per min at 28°C. ␤-Xylosidase activities were determined as previously described using p-nitrophenyl ␤-Dxylopyranoside as substrate (31). Inositol dehydrogenase activities were determined as described (9) by measuring the formation of NADH from NAD plus inositol at 37°C.…”

Section: Methodsmentioning

confidence: 99%

The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression

Galinier

Haiech

Kilhoffer

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

210

274

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Carbon catabolite repression (CCR) of several Bacillus subtilis catabolic genes is mediated by ATPdependent phosphorylation of histidine-containing protein (HPr), a phosphocarrier protein of the phosphoenolpyruvate (PEP): sugar phosphotransferase system. In this study, we report the discovery of a new B. subtilis gene encoding a HPr-like protein, Crh (for catabolite repression HPr), composed of 85 amino acids. Crh exhibits 45% sequence identity with HPr, but the active site His-15 of HPr is replaced with a glutamine in Crh. Crh is therefore not phosphorylated by PEP and enzyme I, but is phosphorylated by ATP and the HPr kinase in the presence of fructose-1,6-bisphosphate. We determined Ser-46 as the site of phosphorylation in Crh by carrying out mass spectrometry with peptides obtained by tryptic digestion or CNBr cleavage. In a B. subtilis ptsH1 mutant strain, synthesis of ␤-xylosidase, inositol dehydrogenase, and levanase was only partially relieved from CCR. Additional disruption of the crh gene caused almost complete relief from CCR. In a ptsH1 crh1 mutant, producing HPr and Crh in which Ser-46 is replaced with a nonphosphorylatable alanyl residue, expression of ␤-xylosidase was also completely relieved from glucose repression. These results suggest that CCR of certain catabolic operons requires, in addition to CcpA, ATP-dependent phosphorylation of Crh, and HPr at Ser-46.The bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) catalyzes the transport and concomitant phosphorylation of carbohydrates via a protein phosphorylation chain including PEP-dependent phosphorylation of His-15 in histidine-containing protein (HPr) by enzyme I (EI). P-His-HPr phosphorylates the sugar-specific EIIAs. In Gram-positive bacteria, the PTS regulates also induction and carbon catabolite repression (CCR) of numerous catabolic genes (1). The central regulatory protein involved in these various functions is HPr. In Gram-positive bacteria, this small phosphoryl transfer protein can be phosphorylated at a regulatory serine (Ser-46) by ATP and the HPr kinase (2, 3), in addition to phosphorylation at the catalytic His-15 by PEP and EI (4, 5). PEP-dependent and ATP-dependent phosphorylation of HPr interfere with each other-i.e., P-His-HPr is a poor substrate for the HPr kinase and P-Ser-HPr is a poor substrate for EI (6, 7). ATP-dependent phosphorylation of HPr is stimulated by glycolytic intermediates such as fructose-1,6-bisphosphate (FBP) in Enterococcus faecalis (6) and in Streptococcus pyogenes (7). It has been reported that FBP is also implicated in CCR of the Bacillus subtilis gnt and iol operons (8, 9), and a potential role of phosphorylation of HPr at Ser-46 in CCR has therefore been investigated (10). The gnt operon contains the genes gntRKPZ encoding the repressor GntR, gluconate kinase, gluconate permease, and a gluconate-6-Pdehydrogenase (11), whereas the iol operon is composed of 10 genes encoding enzymes presumably implicated in inositol metabolism, including iolG encoding inositol dehydro...

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“…On minimal media, B. subtilis ccpA mutant strains exhibit a severe growth defect (12,16,24). This defect is most obvious on minimal media with glucose and ammonia as single sources of carbon and nitrogen, respectively.…”

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confidence: 99%

“…Severe growth defects of B. subtilis ccpA mutants were observed in minimal media. Even in the presence of glutamate and glucose, the growth rate of the ccpA mutant is lower than that of wild-type strains (12). We attempted therefore to identify the factor(s) that is required to allow a growth rate of the ccpA mutant comparable to that of wild-type strains.…”

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confidence: 99%

Insufficient Expression of theilv-leuOperon Encoding Enzymes of Branched-Chain Amino Acid Biosynthesis Limits Growth of aBacillus subtilis ccpAMutant

et al. 2002

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Bacillus subtilis ccpA mutant strains exhibit two distinct phenotypes: they are defective in catabolite repression, and their growth on minimal media is strongly impaired. This growth defect is largely due to a lack of expression of the gltAB operon. However, growth is impaired even in the presence of glutamate. Here, we demonstrate that the ccpA mutant strain needs methionine and the branched-chain amino acids for optimal growth. The control of expression of the ilv-leu operon by CcpA provides a novel regulatory link between carbon and amino acid metabolism.

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Regulation of xylanolytic enzymes in Bacillus subtilis

Cited by 73 publications

References 24 publications

Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene

Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene

The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression

Insufficient Expression of theilv-leuOperon Encoding Enzymes of Branched-Chain Amino Acid Biosynthesis Limits Growth of aBacillus subtilis ccpAMutant

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