Disease relevance of ECs4208

• The restriction fragments carrying the region preceding the Escherichia coli crp structural gene were transcribed [1].
• The gene encoding cAMP receptor protein is required for competence development in Haemophilus influenzae Rd [2].
• Identification and characterization of a novel cAMP receptor protein in the cyanobacterium Synechocystis sp. PCC 6803 [3].
• CooA, a member of the cAMP receptor protein (CRP) family, is a CO-sensing transcription activator from Rhodospirillum rubrum that binds specific DNA sequences in response to CO [4].
• DNA X CRP remains as resistant to attack by subtilisin, clostripain, and the Staphylococcus aureus V8 protease as unliganded CRP but is slowly digested by chymotrypsin [5].

High impact information on ECs4208

• The cAMP receptor protein (CRP) and MaIT, the maltose regulon activator, synergistically activate transcription from the E. coli maIKp promoter [6].
• CRP and RNA polymerase bind to the crp regulatory region simultaneously [1].
• Interactions between catabolite gene activator protein (CAP) and RNA polymerase have been proposed based on face-of-helix-dependent transcription activation by CAP and based on face-of-helix-dependent cooperative binding of CAP and RNA polymerase to promoter DNA [7].
• In the first four operons these DNA sequences closely matched the consensus sequence that binds to the cyclic AMP-receptor protein [8].
• In Escherichia coli the element responsible for cAMP-mediated transcriptional induction is the binding site for the cAMP-receptor protein (CAP) [9].

Chemical compound and disease context of ECs4208

• The 2.9 A resolution crystal structure of Escherichia coli catabolite gene activator protein (CAP) complexed with cyclic AMP reveals two distinct structural domains separated by a cleft [10].
• Glucose causes catabolite repression by lowering the intracellular levels of both cAMP and cAMP receptor protein (CRP) in Escherichia coli [11].
• CooA is a member of a family of transcriptional regulators similar to the cAMP receptor protein and fumavate nitrate reduction from Escherichia coli [12].
• Regulation of bacterial glycogen synthesis. Stimulation of glycogen synthesis by endogenous and exogenous cyclic adenosine 3':5'-monophosphate in Escherichia coli and the requirement for a functional CRP gene [13].
• Escherichia coli NCR91 synthesizes a mutant form of catabolite gene activator protein (CAP) in which alanine 144 is replaced by threonine [14].

Biological context of ECs4208

• In mammalian cells the cAMP regulatory element is composed of one or more binding sites for various transcription factors [9].
• Three mutations that alter the DNA sequence specificity of the catabolite gene activator protein (CAP) from AA-TGTGA--T---TCA-ATW to AA-TGTAA--T---TCA-ATW have been isolated [15].
• Genetic strategy for analyzing specificity of dimer formation: Escherichia coli cyclic AMP receptor protein mutant altered in its dimerization specificity [16].
• Mutations which permit cAMP binding protein (CRP) to act in the absence of cAMP have been isolated by in vitro mutagenesis of a plasmid containing the cloned crp gene [17].
• We have examined the effects of a series of deletions and point mutations in the gal promoter region on CRP binding [18].

Anatomical context of ECs4208

• Comparison of the recently determined amino acid sequences of the regulatory subunit of cAMP-dependent protein kinase (RII) from bovine cardiac muscle and the Escherichia coli catabolite gene activator protein (CAP) shows significant homology [19].
• Nine hybridoma clones producing antibodies against the Escherichia coli cAMP receptor protein (CRP) have been isolated [20].
• We propose that ribosome translation to the crp stop codon causes read-through of the terminator [21].
• It is proposed that an E. coli cell entering stationary phase requires a change in cell envelope structure which involes a cyclic AMP-CRP dependent process, and without this process the permeability of the cell membrane increases [22].

Associations of ECs4208 with chemical compounds

• We show that glucose lowers the level of crp mRNA without affecting its stability [11].
• The structure of complexes formed between cAMP receptor protein (CRP) and various restriction fragments from the promoter region of the lactose operon has been analysed by measurements of electrodichroism [23].
• We have used random mutagenesis and alanine scanning to identify determinants within alphaCTD for transcription activation at a Class II CRP-dependent promoter [24].
• A very high concentration of heparin is able to dissociate CRP from the galP1 ternary complex without changing the properties of the complex [25].
• Adenylate cyclase deficient cells harbouring the mutant (crp*) plasmids exhibited a variety of fermentation profiles on MacConkey indicator plates containing various sugars. beta-galactosidase synthesis in cells carrying the crp* plasmids was activated most by the addition of cGMP as well as cAMP [17].

Other interactions of ECs4208

• It was shown that P. multocida adenylate cyclase synthesizes increased levels of cyclic AMP in E. coli strains deficient in the catabolite gene activator protein compared with wild-type strains [26].

Analytical, diagnostic and therapeutic context of ECs4208

• We have used site-directed mutagenesis to replace amino acid 1 of the recognition alpha-helix of the catabolite gene activator protein (CAP), Arg-180, with glycine and with alanine [27].
• Northern blot analysis revealed that the mRNA for ptsG, a major glucose transporter gene, was markedly reduced in a delta crp or delta cya background [28].
• We have investigated the in vitro interactions of the cAMP receptor protein (CRP).cAMP regulatory complex with two DNA binding sites, by gel mobility-shift assays, and report the analysis of the functional role of each of the binding sites in vivo [29].
• Chromatin immunoprecipitation and high-density microarrays have been used to monitor the distribution of the global transcription regulator Escherichia coli cAMP-receptor protein (CRP) and RNA polymerase along the E. coli chromosome [30].
• Stopped-flow fluorimetry was employed to study the kinetics of the conformational changes in CRP induced by cAMP binding to high and low affinity receptor sites [31].

References