cAMP Receptor Protein from &lt;i&gt;Escherichia coli&lt;/i&gt; as a Model of Signal Transduction in Proteins – A Review

Fic, Ewelina; Bonarek, Piotr; Górecki, Andrzej; Kędracka–Krok, Sylwia; Mikołajczak, Jan; Polit, Agnieszka; Tworzydło, Magdalena; Dziedzicka-Wasylewska, Marta; Wasylewski, Zygmunt

doi:10.1159/000178014

Cited by 80 publications

(79 citation statements)

References 141 publications

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“…Novel regulatory roles of Cra. The most important regulatory role of Cra is believed to be the control of central carbon metabolism (10,38). The newly identified targets were located within the metabolic map (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…One well-characterized regulator of the genes for carbon source utilization is CRP (cyclic AMP [cAMP] receptor protein) (sometimes called catabolite activator protein [CAP]), which is converted into the functional form after binding cAMP that is synthesized in the absence of glucose (10,22). Besides CRP, another transcription factor, Cra (catabolite repressor activator), has been indicated to play a role in the global regulation of the genes for carbon metabolism (16,46).…”

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Novel Members of the Cra Regulon Involved in Carbon Metabolism in Escherichia coli

2011

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Cra (catabolite repressor activator) is a global regulator of the genes for carbon metabolism in Escherichia coli. To gain insights into the regulatory roles of Cra, attempts were made to identify the whole set of regulation targets using an improved genomic SELEX (systematic evolution of ligands by exponential enrichment) system. Surprisingly, a total of 164 binding sites were identified for Cra, 144 (88%) of which were newly identified. The majority of known targets were included in the SELEX chip pattern. The promoters examined by the lacZ reporter assay in vivo were all regulated by Cra. These two lines of evidence indicate that a total of as many as 178 promoters are under the control of Cra. The majority of Cra targets are the genes coding for the enzymes involved in central carbon metabolism, covering all the genes for the enzymes involved in glycolysis and metabolism downstream of glycolysis, including the tricarboxylic acid (TCA) cycle and aerobic respiration. Taken together, we propose that Cra plays a key role in balancing the levels of the enzymes for carbon metabolism.Central carbon metabolism consists of three major pathways, the glycolysis (Embden-Meyerhof-Parnas [EMP]) pathway, the pentose-phosphate (PP) pathway, and the tricarboxylic acid (TCA) cycle, altogether leading to the production of metabolic energy. These three pathways also provide a number of building blocks that are utilized for the construction of cell architecture (for reviews, see references 26, 43, and 50).

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Section: Discussionmentioning

confidence: 99%

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Novel Members of the Cra Regulon Involved in Carbon Metabolism in Escherichia coli

2011

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“…The catabolite repressor protein (CRP) is activated by the alarmone cyclic AMP (cAMP) (13). cAMP is produced by adenylate cyclase (CyaA) in low-glucose environments, leading to activation of CRP (13).…”

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“…cAMP is produced by adenylate cyclase (CyaA) in low-glucose environments, leading to activation of CRP (13). Glucose inhibits E. coli biofilm formation, and ⌬cyaA and ⌬crp laboratory strains have a decreased propensity for biofilm formation, suggesting that cAMP and CRP are important for regulating biofilm development (14,15).…”

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The Catabolite Repressor Protein-Cyclic AMP Complex Regulates csgD and Biofilm Formation in Uropathogenic Escherichia coli

et al. 2016

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The extracellular matrix protects Escherichia coli from immune cells, oxidative stress, predation, and other environmental stresses. Production of the E. coli extracellular matrix is regulated by transcription factors that are tuned to environmental conditions. The biofilm master regulator protein CsgD upregulates curli and cellulose, the two major polymers in the extracellular matrix of uropathogenic E. coli (UPEC) biofilms. We found that cyclic AMP (cAMP) regulates curli, cellulose, and UPEC biofilms through csgD. The alarmone cAMP is produced by adenylate cyclase (CyaA), and deletion of cyaA resulted in reduced extracellular matrix production and biofilm formation. The catabolite repressor protein (CRP) positively regulated csgD transcription, leading to curli and cellulose production in the UPEC isolate, UTI89. Glucose, a known inhibitor of CyaA activity, blocked extracellular matrix formation when added to the growth medium. The mutant strains ⌬cyaA and ⌬crp did not produce rugose biofilms, pellicles, curli, cellulose, or CsgD. Three putative CRP binding sites were identified within the csgD-csgB intergenic region, and purified CRP could gel shift the csgD-csgB intergenic region. Additionally, we found that CRP binded upstream of kpsMT, which encodes machinery for K1 capsule production. Together our work shows that cAMP and CRP influence E. coli biofilms through transcriptional regulation of csgD. IMPORTANCE The catabolite repressor protein (CRP)-cyclic AMP (cAMP) complex influences the transcription of ϳ7% of genes on the Escherichia coli is a multifaceted Gram-negative bacterium that is equipped for survival in disparate environments ranging from the gastrointestinal and urinary tracts to waterways and soil (1). Growth of E. coli can occur with either planktonic or biofilm lifestyles, the transition between which requires a highly organized shift in gene expression. The biofilm lifestyle is characterized by adherence, slow growth, resistance to environmental insults, and production of an extracellular matrix (ECM) (2). CsgD is the major biofilm regulator of E. coli and of many other bacteria of the Enterobacteriaceae family (3-5), and it promotes the production of two E. coli surface appendages, the amyloid fiber curli and the fibrous glycan chain cellulose (2). CsgD represses the transcription of motility-associated genes, while mediating self and surface attachment (6-8).E. coli is found in ϳ80% of urinary tract infections (UTI), more than any other causative agent, and has the ability to thrive in the bladder and urinary tract environments (9). During UTI, uropathogenic E. coli (UPEC) uses various means to evade and colonize the host. Curli and other factors function in establishing an initial bacterial titer (10). Once in the bladder, E. coli utilizes type 1 pili to invade bladder epithelial cells (11). E. coli bacteria then form a biofilm-like structure known as an intracellular bacterial community (IBC), and cells are coated by the ECM component K1 for protection from host cell recognition ...

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“…1B) (20)(21)(22); and it is specifically induced when phenylethylamine (PEA) is provided as a carbon source (20). The fact that Crp regulates this pathway (23,24) indicates that it serves a catabolic role rather than exclusively one of detoxification. Indeed, it has been shown that the pathway can enable E. coli to grow using PEA as the sole carbon source (20).…”

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How Escherichia coli Tolerates Profuse Hydrogen Peroxide Formation by a Catabolic Pathway

Kumar

Imlay

2013

J Bacteriol

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When Escherichia coli grows on conventional substrates, it continuously generates 10 to 15 M/s intracellular H 2 O 2 through the accidental autoxidation of redox enzymes. Dosimetric analyses indicate that scavenging enzymes barely keep this H 2 O 2 below toxic levels. Therefore, it seemed potentially problematic that E. coli can synthesize a catabolic phenylethylamine oxidase that stoichiometrically generates H 2 O 2 . This study was undertaken to understand how E. coli tolerates the oxidative stress that must ensue. Measurements indicated that phenylethylamine-fed cells generate H 2 O 2 at 30 times the rate of glucose-fed cells. Two tolerance mechanisms were identified. First, in enclosed laboratory cultures, growth on phenylethylamine triggered induction of the OxyR H 2 O 2 stress response. Null mutants (⌬oxyR) that could not induce that response were unable to grow. This is the first demonstration that OxyR plays a role in protecting cells against endogenous H 2 O 2 . The critical element of the OxyR response was the induction of H 2 O 2 scavenging enzymes, since mutants that lacked NADH peroxidase (Ahp) grew poorly, and those that additionally lacked catalase did not grow at all. Other OxyR-controlled genes were expendable. Second, phenylethylamine oxidase is an unusual catabolic enzyme in that it is localized in the periplasm. Calculations showed that when cells grow in an open environment, virtually all of the oxidase-generated H 2 O 2 will diffuse across the outer membrane and be lost to the external world, rather than enter the cytoplasm where H 2 O 2 -sensitive enzymes are located. In this respect, the periplasmic compartmentalization of phenylethylamine oxidase serves the same purpose as the peroxisomal compartmentalization of oxidases in eukaryotic cells.

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cAMP Receptor Protein from <i>Escherichia coli</i> as a Model of Signal Transduction in Proteins – A Review

Cited by 80 publications

References 141 publications

Novel Members of the Cra Regulon Involved in Carbon Metabolism in Escherichia coli

Novel Members of the Cra Regulon Involved in Carbon Metabolism in Escherichia coli

The Catabolite Repressor Protein-Cyclic AMP Complex Regulates csgD and Biofilm Formation in Uropathogenic Escherichia coli

How Escherichia coli Tolerates Profuse Hydrogen Peroxide Formation by a Catabolic Pathway

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