Repression of the Gene Encoding Succinate Dehydrogenase in Respon to Glucose Is Mediated by the EIICBGIC Protein in Escherichia coli

Takeda, Shin‐ichiro; Matsushika, Akinori; Mizuno, Takeshi

doi:10.1093/oxfordjournals.jbchem.a022457

Cited by 9 publications

(17 citation statements)

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“…With respect to Spot42, the only known transcription regulator is the catabolic repressor protein (CRP), which represses Spot42 expression when cAMP levels are high (Moller et al 2002b). It has been known for some time that the expression of sdhCDAB mRNA is repressed in the presence of glucose (Park et al 1995;Takeda et al 1999). A role for the CRP-cAMP complex in the regulation of sdhCDAB transcription has been reported (Nam et al 2005).…”

Section: Discussionmentioning

confidence: 99%

Noncanonical repression of translation initiation through small RNA recruitment of the RNA chaperone Hfq

Desnoyers¹,

Massé²

2012

Genes Dev.

122

136

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The RNA chaperone Hfq is mostly known to help small regulatory RNAs (sRNAs) interact with target mRNAs to block initiating ribosomes. In this model, whereas the sRNA is directly competing with initiating 30S ribosomal subunits, Hfq plays only an indirect role, allowing optimal sRNA-mRNA pairing. Here we report that Hfq is recruited by a sRNA, Spot42, to bind to a precise AU-rich region in the vicinity of the translation initiation region (TIR) of sdhC mRNA and competes directly with 30S ribosomal subunits. We show that the sRNA Spot42 binds sdhC too far upstream of the TIR to directly repress translation initiation in vitro and in vivo. Contrary to the canonical model of sRNA regulation, this suggests a new mechanism where Hfq is directly involved in the translational repression of the target mRNA and where the sRNA acts only as a recruitment factor.

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Section: Discussionmentioning

confidence: 99%

Noncanonical repression of translation initiation through small RNA recruitment of the RNA chaperone Hfq

Desnoyers¹,

Massé²

2012

Genes Dev.

122

136

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“…With respect to succinate production, loss of a functional EIICB glc might similarly allow expression of enzymes normally repressed in the presence of glucose that could be crucial to the fermentation. EIICB glc has recently been proposed to have regulatory functions itself as well, including a direct effect on the expression of several genes, including its own regulatory gene, and possibly a role as a global sensor of glucose (8,24,30).…”

Section: Discussionmentioning

confidence: 99%

Mutation of the ptsG Gene Results in Increased Production of Succinate in Fermentation of Glucose by Escherichia coli

Chatterjee

Millard

Champion

et al. 2001

Appl Environ Microbiol

200

125

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Escherichia coli NZN111 is blocked in the ability to grow fermentatively on glucose but gave rise spontaneously to a mutant that had this ability. The mutant carries out a balanced fermentation of glucose to give approximately 1 mol of succinate, 0.5 mol of acetate, and 0.5 mol of ethanol per mol of glucose. The causative mutation was mapped to the ptsG gene, which encodes the membrane-bound, glucose-specific permease of the phosphotransferase system, protein EIICB glc . Replacement of the chromosomal ptsG gene with an insertionally inactivated form also restored growth on glucose and resulted in the same distribution of fermentation products. The physiological characteristics of the spontaneous and null mutants were consistent with loss of function of the ptsG gene product; the mutants possessed greatly reduced glucose phosphotransferase activity and lacked normal glucose repression. Introduction of the null mutant into strains not blocked in the ability to ferment glucose also increased succinate production in those strains. This phenomenon was widespread, occurring in different lineages of E. coli, including E. coli B.

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“…The process does not involve Mlc directly (439) control sdh-suc transcription directly (339). Apparently, another global carbon regulator, Cra (also known as FruR), also is not involved (339).…”

Section: Limiting the Tricarboxylic Acid Cyclementioning

confidence: 96%

“…The mechanism that causes glucose repression, and thus the Crabtree effect, is less clear. Glucose represses sdh-suc indirectly through the action of EIICB(Glc), but the mechanism remains a mystery (439). The membrane-bound EIICB (Glc), part of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS), phosphorylates and translocates glucose.…”

Section: Limiting the Tricarboxylic Acid Cyclementioning

confidence: 99%

“…Whereas Cra positively regulates the genes that encode the GB and gluconeogenesis (319,366,389,439), there exists no evidence that this global regulator exerts a significant effect on acs transcription (Beatty and Wolfe, unpublished). Finally, no evidence supports a role for arp, a putative gene predicted to encode an ankyrin-like protein and mistakenly annotated as an ACS regulatory protein (Beatty and Wolfe, unpublished).…”

Section: Other Regulatory Factorsmentioning

confidence: 99%

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The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,082

1,274

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To succeed, many cells must alternate between life-styles that permit rapid growth in the presence of abundant nutrients and ones that enhance survival in the absence of those nutrients. One such change in life-style, the “acetate switch,” occurs as cells deplete their environment of acetate-producing carbon sources and begin to rely on their ability to scavenge for acetate. This review explains why, when, and how cells excrete or dissimilate acetate. The central components of the “switch” (phosphotransacetylase [PTA], acetate kinase [ACK], and AMP-forming acetyl coenzyme A synthetase [AMP-ACS]) and the behavior of cells that lack these components are introduced. Acetyl phosphate (acetyl∼P), the high-energy intermediate of acetate dissimilation, is discussed, and conditions that influence its intracellular concentration are described. Evidence is provided that acetyl∼P influences cellular processes from organelle biogenesis to cell cycle regulation and from biofilm development to pathogenesis. The merits of each mechanism proposed to explain the interaction of acetyl∼P with two-component signal transduction pathways are addressed. A short list of enzymes that generate acetyl∼P by PTA-ACKA-independent mechanisms is introduced and discussed briefly. Attention is then directed to the mechanisms used by cells to “flip the switch,” the induction and activation of the acetate-scavenging AMP-ACS. First, evidence is presented that nucleoid proteins orchestrate a progression of distinct nucleoprotein complexes to ensure proper transcription of its gene. Next, the way in which cells regulate AMP-ACS activity through reversible acetylation is described. Finally, the “acetate switch” as it exists in selected eubacteria, archaea, and eukaryotes, including humans, is described

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Repression of the Gene Encoding Succinate Dehydrogenase in Respon to Glucose Is Mediated by the EIICBGIC Protein in Escherichia coli

Cited by 9 publications

References 0 publications

Noncanonical repression of translation initiation through small RNA recruitment of the RNA chaperone Hfq

Noncanonical repression of translation initiation through small RNA recruitment of the RNA chaperone Hfq

Mutation of the ptsG Gene Results in Increased Production of Succinate in Fermentation of Glucose by Escherichia coli

The Acetate Switch

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