Regulation of the sacPA operon of Bacillus subtilis: identification of phosphotransferase system components involved in SacT activity

Arnaud, Maryvonne; Vary, Patricia S.; Zagorec, Monique; Klier, André; Débarbouillé, Michel; Postma, P.; Rapoport, Georges

doi:10.1128/jb.174.10.3161-3170.1992

Cited by 77 publications

(76 citation statements)

References 46 publications

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“…4; compare lanes 6 -27 Ϫ/ϩbglF, respectively, with lanes 4 and 5). No phosphorylation by HPr could be detected for the proteins with exchanges C76R, S97P, H101L, E153V, and H160R (lanes 6,12,20,24,26), and signals were extremely reduced with the mutants carrying exchanges of I80 and D100 (lanes 8, 14,16,18). Surprisingly, when cells expressed the Q91R protein, an additional phosphorylated band appeared approximately 3 kDa above the phosphorylated GalK-BglG fusion protein (lanes 10 and 11).…”

Section: Eii Bgl In Addition Contributed To Its Phosphorylation (Lanementioning

confidence: 96%

Regulation of the Escherichia coli Antiterminator Protein BglG by Phosphorylation at Multiple Sites and Evidence for Transfer of Phosphoryl Groups between Monomers

Görke

2003

Journal of Biological Chemistry

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Activity of antiterminator protein BglG regulating the ␤-glucoside operon in Escherichia coli is controlled by the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) in a dual manner. It requires HPr phosphorylation to be active, whereas phosphorylation by the ␤-glucoside-specific transport protein EII Bgl inhibits its activity. BglG and its relatives carry two PTS regulation domains (PRD1 and PRD2), each containing two conserved histidines. For BglG, histidine 208 in PRD2 was reported to be the negative phosphorylation site. In contrast, other antiterminators of this family are negatively regulated by phosphorylation of the first histidine in PRD1, and presumably activated by phosphorylation of the histidines in PRD2. In this work, a screen for mutant BglG proteins that escape repression by EII Bgl yielded exchanges of nine residues within PRD1, including conserved histidines His-101 and His-160, and C-terminally truncated proteins. Genetic and phosphorylation analyses indicate that His-101 in PRD1 is phosphorylated by EII Bgl and that His-160 contributes to negative regulation. His-208 in PRD2 is essential for BglG activity, suggesting that it is phosphorylated by HPr. Surprisingly, phosphorylation by HPr is not fully abolished by exchanges of His-208. However, phosphorylation by HPr is inhibited by exchanges in PRD1 and the phosphorylation of these mutants is restored in the presence of wild-type BglG. These results suggest that the activating phosphoryl group is transiently donated from HPr to PRD1 and subsequently transferred to His-208 of a second BglG monomer. The active His-208-phosphorylated BglG dimer can subsequently be inhibited in its activity by EII Bgl -catalyzed phosphorylation at His-101.

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Section: Eii Bgl In Addition Contributed To Its Phosphorylation (Lanementioning

confidence: 96%

Regulation of the Escherichia coli Antiterminator Protein BglG by Phosphorylation at Multiple Sites and Evidence for Transfer of Phosphoryl Groups between Monomers

Görke

2003

Journal of Biological Chemistry

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“…In addition, the sacPA and the bglPH operons are subject to catabolite repression. The antiterminators controlling the expression of these operons depend on a stimulation by HPr to be active, in addition to negative control exerted by the specific EII (Arnaud et al, 1992;Le Coq et al, 1995). The levanase operon, which encodes a fructosespecific PTS (lev-PTS) and an extracellular enzyme, levanase, is positively regulated by a NifA-like activator protein, LevR.…”

Section: Introductionmentioning

confidence: 99%

Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT

Stülke

Martin‐Verstraete

Zagorec³

et al. 1997

Molecular Microbiology

165

187

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SummaryGlucose is the preferred carbon and energy source of Bacillus subtilis. It is transported into the cell by the glucose-specific phosphoenolpyruvate:sugar phosphotransferase system (PTS) encoded by the ptsGHI locus. We show here that these three genes (ptsG, ptsH, and ptsI ) form an operon, the expression of which is inducible by glucose. In addition, ptsH and ptsI form a constitutive ptsHI operon. The promoter of the ptsGHI operon was mapped and expression from this promoter was found to be constitutive. Deletion mapping of the promoter region revealed the presence of a transcriptional terminator as a regulatory element between the promoter and coding region of the ptsG gene. Mutations within the ptsG gene were characterized and their consequences on the expression of ptsG studied. The results suggest that expression of the ptsGHI operon is subject to negative autoregulation by the glucose permease, which is the ptsG gene product. A regulatory gene located upstream of the ptsGHI operon, termed glcT, was also identified. The GlcT protein is a novel member of the BglG family of transcriptional antiterminators and is essential for the expression of the ptsGHI operon. A deletion of the terminator alleviates the need for GlcT. The activity of GlcT is negatively regulated by the glucose permease.

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“…Some antiterminators from Gram-positive bacteria were shown to be activated by HPr-catalyzed phosphorylation on one or more of the conserved histidines (13,15,16). The HPr-catalyzed phosphorylation was proposed to be part of a mechanism of carbon catabolite repression (CCR) that operates in Gram-positive bacteria (reviewed in ref.…”

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confidence: 99%

Modulation of transcription antitermination in the bgl operon of Escherichia coli by the PTS

Raveh¹,

Lopian²,

Nussbaum-Shochat³

et al. 2009

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

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BglG, which regulates expression of the ␤-glucoside utilization (bgl) operon in Escherichia coli, represents a family of RNA-binding transcriptional antiterminators that positively regulate transcription of sugar utilization genes in Gram-negative and Gram-positive organisms. BglG is negatively regulated by the ␤-glucoside phosphotransferase, BglF, by means of phosphorylation and physical association, and it is positively regulated by the general phosphoenolpyruvate phosphotransferase system (PTS) proteins, enzyme I (EI) and HPr. We studied the positive regulation of BglG both in vitro and in vivo. Here, we show that although EI and HPr are essential for BglG activity, this mode of activation does not require phosphorylation of BglG by HPr, as opposed to the phosphorylation-mediated activation of many BglG-like antiterminators in Gram-positive organisms. The effect of EI and HPr on BglG is not mediated by BglF. Nevertheless, the release of BglG from BglF, which is stimulated by the extracellular sugar in a sugar uptakeindependent manner, is a prerequisite for BglG activation. Taken together, the results indicate that activation of BglG is a 2-stage process: a sugar-stimulated release from the membrane-bound sugar sensor followed by a phosphorylation-independent stimulatory effect exerted by the general PTS proteins.bgl system ͉ E. coli

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Regulation of the sacPA operon of Bacillus subtilis: identification of phosphotransferase system components involved in SacT activity

Cited by 77 publications

References 46 publications

Regulation of the Escherichia coli Antiterminator Protein BglG by Phosphorylation at Multiple Sites and Evidence for Transfer of Phosphoryl Groups between Monomers

Regulation of the Escherichia coli Antiterminator Protein BglG by Phosphorylation at Multiple Sites and Evidence for Transfer of Phosphoryl Groups between Monomers

Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT

Modulation of transcription antitermination in the bgl operon of Escherichia coli by the PTS

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