Identification of a second β-glucoside phosphoenolpyruvate : carbohydrate phosphotransferase system in Corynebacterium glutamicum R

Tanaka, Yoshihiko; Teramoto, Haruhiko; Inui, Masayuki; Yukawa, Hideaki

doi:10.1099/mic.0.029496-0

Cited by 16 publications

(15 citation statements)

References 32 publications

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“…In the C. glutamicum ATCC 13032 strain, disruption of ptsG alone resulted in the marked decrease of glucose consumption (28,29), in contrast to the high glucose utilization ability remaining in the C. glutamicum R ptsG-deficient strain. This is explained by the presence of disrupted bgl PTS genes found in the C. glu- tamicum ATCC 13032 genome (41). The residual glucose transport observed in the ptsG-deficient strain derived from C. glutamicum ATCC 13032 and the ptsG bglF bglF2 triple deletion strain from C. glutamicum R may indicate the presence of another minor glucose transporter.…”

Section: Discussionmentioning

confidence: 98%

“…Glucose exerts repression mainly at the antitermination step of expression of the bglF gene cluster. Whether glucose affects expression of the bglF gene cluster at transcription antitermination was investigated by using the bglF promoter-lacZ reporter system (41). The bglF promoter-lacZ (bglF-lacZ) and bglF2 promoter-lacZ (bglF2-lacZ) fusions were integrated into the chromosome of wild-type C. glutamicum.…”

Section: Methodsmentioning

confidence: 99%

“…bglG and bglG2 encode members of transcriptional antiterminator BglG/ SacY family. Expression of both bglF and bglF2 is regulated via the antitermination mechanism dependent on BglG and BglG2, respectively (41). Interestingly, bglF and bglF2 show different expression patterns in the presence of glucose.…”

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confidence: 99%

“…glutamicum strains ATCC 13032 and ATCC 13869, it is capable of utilizing ␤-glucosides (24,41). C. glutamicum R has two ␤-glucoside utilization gene clusters, bglF-bglA-bglG and bglF2-bglA2-bglG2 (Fig.…”

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Translation Efficiency of Antiterminator Proteins Is a Determinant for the Difference in Glucose Repression of Two β-Glucoside Phosphotransferase System Gene Clusters inCorynebacterium glutamicumR

et al. 2011

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Corynebacterium glutamicum R has two ␤-glucoside phosphoenolpyruvate, carbohydrate phosphotransferase systems (PTS) encoded by bglF and bglF2 located in the respective clusters, bglF-bglA-bglG and bglF2-bglA2-bglG2. Previously, we reported that whereas ␤-glucoside-dependent induction of bglF is strongly repressed by glucose, glucose repression of bglF2 is very weak. Here, we reveal the mechanism behind the different effects of glucose on the two bgl genes. Deletion of the ribonucleic antiterminator sequence and transcriptional terminator located upstream of the translation initiation codon of bglF markedly relieved the glucose repression of a bglF-lacZ fusion, indicating that glucose affects the antitermination mechanism that is responsible for the ␤-glucoside-dependent induction of the bglF cluster. The glucose repression of bglF mRNA was also relieved by introducing a multicopy plasmid carrying the bglG gene encoding an antiterminator of the bglF cluster. Moreover, replacement of the GUG translation initiation codon of bglG with AUG was effective in relieving the glucose repression of bglF and bglG. Inversely, expression of bglF2 and bglG2 was subject to strict glucose repression in a mutant strain in which the AUG translation initiation codon of bglG2 encoding antiterminator of the bglF2 cluster was replaced with GUG. These results suggest that the translation initiation efficiency of the antiterminator proteins, at least in part, determines whether the target genes are subject to glucose repression. We also found that bglF expression was induced by glucose in the BglG-overexpressing strains, which may be explained by the ability of BglF to transport glucose.In many bacterial cells, ␤-glucosides are taken up via the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS), which is consequently important for the acquisition of various carbohydrates (22, 34). The PTS consists of two common cytoplasmic proteins, enzyme I (EI) and HPr, and an array of carbohydrate-specific enzyme II (EII) permeases. The phosphoryl group from phosphoenolpyruvate is sequentially transferred to EI, HPr, EII, and finally to the carbohydrate as it is translocated across the membrane.An antitermination mechanism has a pivotal role in regulation of ␤-glucoside PTS genes in many bacteria. The regulation has been well studied in Escherichia coli and Bacillus subtilis. In the antitermination regulatory mechanism, transcription stops at a terminator sequence present in the 5Ј untranslated region (UTR) of the target mRNA. In the presence of substrate sugar, a transcriptional antiterminator protein of the BglG/ SacY family binds to the ribonucleic antiterminator (RAT) sequence partially overlapping the transcriptional terminator and thereby results in transcription elongation to the end of the target gene (1,5,38).An antiterminator such as E. coli BglG or B. subtilis LicT is inactivated by phosphorylation at the PTS regulation domain 1 (PRD-1) by a ␤-glucoside EII. Concomitant with PTS-dependent uptake and phosphorylation of the subs...

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Section: Discussionmentioning

confidence: 98%

Section: Methodsmentioning

confidence: 99%

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Translation Efficiency of Antiterminator Proteins Is a Determinant for the Difference in Glucose Repression of Two β-Glucoside Phosphotransferase System Gene Clusters inCorynebacterium glutamicumR

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“…Our study showed the presence of posttranscriptional regulation mediated by mRNA binding protein in this industrially important microorganism, and these examples should be expanded in the near future (27,28).…”

Section: Discussionmentioning

confidence: 99%

Regulation of the Expression of De Novo Pyrimidine Biosynthesis Genes in Corynebacterium glutamicum

2015

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Expression of pyrimidine de novo biosynthesis is downregulated by an exogenous uracil in many bacteria. In this study, we show that a putative binding motif sequence of PyrR is required for uracil-mediated repression of pyrR-lacZ translational fusion. However, the uracil response was still observed in the strain with the pyrR gene deleted, implying the existence of a uracil response factor other than PyrR which also acts through the PyrR binding loop region. Deletion of rho, encoding the transcription termination factor Rho, resulted in an increase in the expression of pyrR-lacZ. Moreover, the strain with a double deletion of pyrR and rho showed elimination of the uracil-responsive downregulation of the pyrR-lacZ. Therefore, expression of the pyrimidine biosynthetic gene cluster in Corynebacterium glutamicum is controlled by two different mechanisms mediated by PyrR and Rho. IMPORTANCEThe pyr genes of C. glutamicum are downregulated in the presence of uracil in culture medium. The mRNA binding regulator PyrR represses the expression of pyr genes, as reported previously. However, the uracil response was still observed in the pyrR deletion strain. Deletion of rho in addition to pyrR deletion results in the elimination of the uracil response. Therefore, we identified the factors that are involved in the uracil response. Involvement of Rho in the regulation of pyrimidine de novo biosynthesis genes has not been reported. Pyrimidine de novo biosynthesis starts with the synthesis of a pyrimidine ring assembled from aspartate, bicarbonate, and glutamine (Fig. 1C). The pyrimidine ring reacts with phosphoribosyl pyrophosphate (PRPP) to generate orotidine 5=-monophosphate (OMP). Subsequently, decarboxylation of OMP results in the formation of UMP, which is converted to other essential pyrimidine nucleotides. Carbamoyl phosphate is also used for biosynthesis of arginine, connecting the pyrimidine biosynthesis with arginine biosynthesis. The pyrimidine-biosynthetic pathway consists of six enzymatic steps, and the genes coding for these enzymes (carA, carB, pyrB, pyrC, pyrD, pyrE, and pyrF) are widely conserved in bacteria (1).Regulation of the expression of pyrimidine de novo biosynthesis genes has been well studied in Escherichia coli and Bacillus subtilis. Many regulatory mechanisms that are not dependent on DNA-binding transcriptional regulators have been demonstrated. Expression of the pyrBI operons in E. coli is proposed to be controlled by transcriptional attenuation (2-4). The regulation at the transcription initiation step has also been reported. In the presence of high concentrations of UTP, nascent transcript slips from the template DNA at the consecutive T residues, resulting in the reiterative addition of UTP to the transcript (5). In B. subtilis, pyrimidine de novo biosynthesis genes are clustered (pyr operon). Expression of the pyr operon is regulated by the transcriptional termination-antitermination mechanism involving the RNAbinding protein PyrR (6, 7). In the absence of PyrR, formation of the antit...

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Global Transcriptional Regulators Involved in Carbon, Nitrogen, Phosphorus, and Sulfur Metabolisms in Corynebacterium glutamicum

Toyoda

Inui

2020

Microbiology Monographs

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Identification of a second β-glucoside phosphoenolpyruvate : carbohydrate phosphotransferase system in Corynebacterium glutamicum R

Cited by 16 publications

References 32 publications

Translation Efficiency of Antiterminator Proteins Is a Determinant for the Difference in Glucose Repression of Two β-Glucoside Phosphotransferase System Gene Clusters inCorynebacterium glutamicumR

Translation Efficiency of Antiterminator Proteins Is a Determinant for the Difference in Glucose Repression of Two β-Glucoside Phosphotransferase System Gene Clusters inCorynebacterium glutamicumR

Regulation of the Expression of De Novo Pyrimidine Biosynthesis Genes in Corynebacterium glutamicum

Global Transcriptional Regulators Involved in Carbon, Nitrogen, Phosphorus, and Sulfur Metabolisms in Corynebacterium glutamicum

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