Klebsiella aerogenes catabolite gene activator protein and the gene encoding it (crp)

Osuna, Robert; Bender, R.

doi:10.1128/jb.173.20.6626-6631.1991

Cited by 11 publications

(5 citation statements)

References 29 publications

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“…This 972 nucleotide open reading frame has coding sequence for a protein of 324 residues which differs from the S. typhimurium and E. coli CysB proteins in only 15 and 21 positions respectively; most of the amino acid replacements are conservative. This degree of sequence identity among homologous proteins from the three species is lower than that observed for the catabolite activator protein (Osuna and Bender, 1991), but significantly higher than that observed between the 8-galactosidase genes of K. aerogenes and E. coli (Buvinger and Riley, 1985).…”

Section: Resultscontrasting

confidence: 55%

Characterization of the CysB protein of Klebsiella aerogenes: direct evidence that N-acetylserine rather than O-acetylserine serves as the inducer of the cysteine regulon

Lynch

Tyrrell

Smerdon

et al. 1994

Biochemical Journal

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The cysB gene of Klebsiella aerogenes has been cloned, sequenced and shown to complement the cysteine auxotrophic phenotype of Escherichia coli cysB mutants. The K. aerogenes cysB gene is predicted to encode a protein of 324 amino acid residues that shares approx. 95% sequence similarity with the Salmonella typhimurium and E. coli CysB proteins. Gel-retardation assays demonstrate that the purified protein binds to DNA fragments containing either the K. aerogenes cysb promoter or the S. typhimurium cysJIH promoter. Acetylserine enhances CysB binding to the cysJIH promoter fragment while diminishing its binding to the cysB promoter fragment. Fluorescence-emission-spectroscopy measurements suggest strongly that N-acetylserine binds to CysB apoprotein but that O-acetylserine does not, and support the notion that N-acetylserine is the physiological inducer of cysteine biosynthesis.

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Section: Resultscontrasting

confidence: 55%

Characterization of the CysB protein of Klebsiella aerogenes: direct evidence that N-acetylserine rather than O-acetylserine serves as the inducer of the cysteine regulon

Lynch

Tyrrell

Smerdon

et al. 1994

Biochemical Journal

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“…Addition of cAMP to the growth medium overcomes glucose-mediated catabolite repression of histidase formation in K. pneumoniae (124). Mutants defective in the genes for adenylate cyclase (cya) or CRP (crp) cannot activate hut expression in response to carbon limitation (115,124). In vitro transcription with purified components showed that both CRP and cAMP were necessary (and sufficient) to activate transcription from hutUp, the hutU promoter (115,116).…”

Section: Enteric Bacteriamentioning

confidence: 99%

“…Mutants defective in the genes for adenylate cyclase (cya) or CRP (crp) cannot activate hut expression in response to carbon limitation (115,124). In vitro transcription with purified components showed that both CRP and cAMP were necessary (and sufficient) to activate transcription from hutUp, the hutU promoter (115,116). The hutUp region contains two CRP-cAMP-binding sites: a stronger site centered at position Ϫ82.5 (relative to the start of transcription) and a weaker site centered at position Ϫ42.5 (116,117).…”

Section: Enteric Bacteriamentioning

confidence: 99%

Regulation of the Histidine Utilization (Hut) System in Bacteria

Bender

2012

Microbiol Mol Biol Rev

125

128

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SUMMARY The ability to degrade the amino acid histidine to ammonia, glutamate, and a one-carbon compound (formate or formamide) is a property that is widely distributed among bacteria. The four or five enzymatic steps of the pathway are highly conserved, and the chemistry of the reactions displays several unusual features, including the rearrangement of a portion of the histidase polypeptide chain to yield an unusual imidazole structure at the active site and the use of a tightly bound NAD molecule as an electrophile rather than a redox-active element in urocanase. Given the importance of this amino acid, it is not surprising that the degradation of histidine is tightly regulated. The study of that regulation led to three central paradigms in bacterial regulation: catabolite repression by glucose and other carbon sources, nitrogen regulation and two-component regulators in general, and autoregulation of bacterial regulators. This review focuses on three groups of organisms for which studies are most complete: the enteric bacteria, for which the regulation is best understood; the pseudomonads, for which the chemistry is best characterized; and Bacillus subtilis , for which the regulatory mechanisms are very different from those of the Gram-negative bacteria. The Hut pathway is fundamentally a catabolic pathway that allows cells to use histidine as a source of carbon, energy, and nitrogen, but other roles for the pathway are also considered briefly here.

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“…The resulting 655-bp product was cloned into the expression vector pET24b with the restriction sites that had been introduced with the primers. Sequence analysis of two of the resulting pET-CRP plasmids revealed two positions that differed from the published sequence of K. aerogenes crp (29). These differences did not cause a change at the protein level, however.…”

Section: Vol 183 2001 Catabolite Repression Of Citrate Fermentationmentioning

confidence: 84%

“…6). It should be mentioned that a very small proportion of the purified protein was probably E. coli CRP, which differs, however, from K. pneumoniae CRP in only one position (29). The corresponding proteins were shown to be completely interchangeable with respect to activation of the E. coli lacZ and the K. pneumoniae hutU promoters (30).…”

Section: Vol 183 2001 Catabolite Repression Of Citrate Fermentationmentioning

confidence: 97%

Catabolite Repression of the Citrate Fermentation Genes in Klebsiella pneumoniae : Evidence for Involvement of the Cyclic AMP Receptor Protein

2001

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Klebsiella pneumoniae is able to grow anaerobically with citrate as a sole carbon and energy source by a fermentative pathway involving the Na ؉ -dependent citrate carrier CitS, citrate lyase, and oxaloacetate decarboxylase. The corresponding genes are organized in the divergent citC and citS operons, whose expression is strictly dependent on the citrate-sensing CitA-CitB two-component system. Evidence is provided here that the citrate fermentation genes are subject to catabolite repression, since anaerobic cultivation with a mixture of citrate and glucose or citrate and gluconate resulted in diauxic growth. Glucose, gluconate, and also glycerol decreased the expression of a chromosomal citS-lacZ fusion by 60 to 75%, whereas a direct inhibition of the citrate fermentation enzymes was not observed. The purified cyclic AMP (cAMP) receptor protein (CRP) of K. pneumoniae bound to two sites in the citC-citS intergenic region, which were centered at position ؊41.5 upstream of the citC and citS transcriptional start sites. Binding was apparently stimulated by the response regulator CitB. These data indicate that catabolite repression of the citrate fermentation genes is exerted by CRP and that in the absence of repressing carbon sources the cAMP-CRP complex serves to enhance the basal, CitB-dependent transcription level.Klebsiella pneumoniae, a member of the Enterobacteriaceae, is able to grow with citrate as a sole carbon and energy source under anoxic conditions (for a review, see reference 4). Citrate fermentation involves uptake by a Na ϩ -dependent citrate carrier (32, 44), cleavage into acetate and oxaloacetate by citrate lyase, and decarboxylation of oxaloacetate to pyruvate by the Na ϩ ion pump oxaloacetate decarboxylase (12, 13). The conversion of pyruvate to acetate, formate, CO 2 , and H 2 (7, 38) is catalyzed by enzymes generally involved in anaerobic pyruvate catabolism. The citrate-specific fermentation genes form a cluster of two divergent operons (5, 6). The citCDEFG operon encodes citrate lyase ligase (CitC), the citrate lyase subunits (CitD, CitE, and CitF), and triphosphoribosyl-dephospho-coenzyme A synthase (CitG), which catalyzes the formation of a precursor of the citrate lyase prosthetic group (36, 37). The citS-oadGAB-citAB operon encodes the citrate carrier CitS, the oxaloacetate decarboxylase subunits (OadG, OadA, and OadB), and a two-component system composed of the sensor kinase CitA and the response regulator CitB (Fig. 1A). The CitA-CitB system was shown to be essential for the expression of both operons (6). CitA presumably functions as a sensor of extracellular citrate, since the periplasmic domain of this membrane-bound protein binds citrate with high affinity (K d Ϸ 6 M) and specificity (23). CitB acts as a transcriptional activator of the citS and the citC operons and binds to two sites in the 193-bp citC-citS intergenic region (Fig. 1) in a phosphorylation-dependent fashion (24).Maximal expression of a chromosomally integrated translational citSЈ-ЈlacZ fusion requires citrate, anoxic...

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Klebsiella aerogenes catabolite gene activator protein and the gene encoding it (crp)

Cited by 11 publications

References 29 publications

Characterization of the CysB protein of Klebsiella aerogenes: direct evidence that N-acetylserine rather than O-acetylserine serves as the inducer of the cysteine regulon

Characterization of the CysB protein of Klebsiella aerogenes: direct evidence that N-acetylserine rather than O-acetylserine serves as the inducer of the cysteine regulon

Regulation of the Histidine Utilization (Hut) System in Bacteria

Catabolite Repression of the Citrate Fermentation Genes in Klebsiella pneumoniae : Evidence for Involvement of the Cyclic AMP Receptor Protein

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