Induction of the nag regulon of Escherichia coli by N-acetylglucosamine and glucosamine: role of the cyclic AMP-catabolite activator protein complex in expression of the regulon

@article{Plumbridge1990InductionOT,
  title={Induction of the nag regulon of Escherichia coli by N-acetylglucosamine and glucosamine: role of the cyclic AMP-catabolite activator protein complex in expression of the regulon},
  author={J. Plumbridge},
  journal={Journal of Bacteriology},
  year={1990},
  volume={172},
  pages={2728 - 2735}
}
  • J. Plumbridge
  • Published 1990
  • Medicine, Biology
  • Journal of Bacteriology
The divergent nag regulon located at 15.5 min on the Escherichia coli map encodes genes necessary for growth on N-acetylglucosamine and glucosamine. Full induction of the regulon requires both the presence of N-acetylglucosamine and a functional cyclic AMP (cAMP)-catabolite activator protein (CAP) complex. Glucosamine produces a lower level of induction of the regulon. A nearly symmetric consensus CAP-binding site is located in the intergenic region between nagE (encoding EIINag) and nagB… Expand
Repression and induction of the nag regulon of Escherichia coll K‐12: the roles of nagC and nagA in maintenance of the uninduced state
TLDR
N‐acetylglucosamine‐6‐phosphate, the intra‐cellular product of N‐acetyglucOSamine transport and the substrate of the nagA gene product, is shown to be an inducer of the regulon and this suggests how nagC mutations result in derepression. Expand
Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS
TLDR
The mlc gene is shown to be allelic with the previously characterized dgsA mutation affecting the mannose phosphoenolpyruvate‐dependent phosphotransferase system (PTS), suggesting that this protein is a more important regulator of manX expression than NagC. Expand
Allosteric Regulation of Glucosamine-6-Phosphate Deaminase (NagB) and Growth of Escherichia coli on Glucosamine
TLDR
Wild-type NagB behaves as if it is already fully allosterically activated during growth on GlcN, and evidence is presented suggesting that sufficient GlcNAc6P for allosteric activation is derived from the recycling of peptidoglycan. Expand
CAP and Nag repressor binding to the regulatory regions of the nagE-B and manX genes of Escherichia coli.
TLDR
Two binding sites have been detected, overlapping the promoters of the nagE and nagB genes, supporting a model where the NagC proteins bind co-operatively to these two sites on the DNA and interact to form a DNA loop. Expand
Co‐ordinated regulation of amino sugar biosynthesis and degradation: the NagC repressor acts as both an activator and a repressor for the transcription of the glmUS operon and requires two separated NagC binding sites.
TLDR
The location of the distal NagC site suggests that this site is behaving like an upstream activating sequence (UAS) and implies that NagC is playing the role of activator for this promoter. Expand
Why Does Escherichia coli Grow More Slowly on Glucosamine than on N-Acetylglucosamine? Effects of Enzyme Levels and Allosteric Activation of GlcN6P Deaminase (NagB) on Growth Rates
TLDR
It was found that for strains carrying a wild-type deaminase (nagB) gene, increasing the level of the NagB protein or the rate of GlcN uptake increased the growth rate, which showed that both enzyme induction and sugar transport were limiting. Expand
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TLDR
Results strongly support the notion that GalNAc uptake depends on a specific phosphotransferase system and show that E. coli K92 has developed a regulation mechanism that specifically induces the appropriate permease based on the presence of each respective phospho-amino sugar. Expand
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TLDR
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TLDR
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  • Biology, Medicine
  • Microbiological reviews
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TLDR
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TLDR
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