On the specificity of cyclic AMP action in <i>Escherichia coli</i>

Pačes, Václav; Smrž, J.

doi:10.1016/0014-5793(73)80137-1

FEBS Letters

1973

DOI: 10.1016/0014-5793(73)80137-1

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On the specificity of cyclic AMP action in Escherichia coli

Václav Pačes

J. Smrž

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2007

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Cited by 2 publications

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“…In cAMP receptor protein-associated cAMP-binding domains, cAMP binds in an anti conformation with the base oriented away from the sugar phosphate, while in many eukaryotic cAMP-binding domains, cAMP binds predominantly in a syn conformation with the base oriented over the sugar phosphate (21,23). The cAMP analog 8-Br-cAMP, which adopts a syn conformation, can therefore be used to preferentially activate eukaryotic protein kinase A (PKA)-like cAMPbinding domains over prokaryotic cAMP receptor protein-like cAMP-binding domains (18,20). Interestingly, the addition of 8-Br-cAMP to cultures of cya crp double mutants transformed with NasP restored the ability of these cultures to produce N-acyl amino acids.…”

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Cyclic AMP Directly Activates NasP, an N -Acyl Amino Acid Antibiotic Biosynthetic Enzyme Cloned from an Uncultured β-Proteobacterium

Clardy

2007

J Bacteriol

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The cyclic AMP (cAMP)-dependent biosynthesis of N-acylphenylalanine antibiotics by NasP, an environmental DNA-derived N-acyl amino acid synthase, is controlled by an NasP-associated cyclic nucleotide-binding domain and is independent of the global cAMP signal transducer, cAMP receptor protein. A 16S rRNA gene sequence found on the same environmental DNA cosmid as NasP is most closely related to 16S sequences from ␤-proteobacteria.

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Cyclic AMP Directly Activates NasP, an N -Acyl Amino Acid Antibiotic Biosynthetic Enzyme Cloned from an Uncultured β-Proteobacterium

Clardy

2007

J Bacteriol

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Investigations on stimulation of lac transcription in vivo in Escherichia coli by cAMP analogues

Scholübbers

Knippenberg

Baraniak

et al. 1984

European Journal of Biochemistry

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The ability of 24 systematically modified analogues of adenosine 3',5'-monophosphate (CAMP) to enhance the synthesis of j?-galactosidase in glucose-repressed Escherichia coli strains KNBL 1001 and cpd-Crookes has been investigated. The properties of the analogues in comparison with cAMP are, with only two exceptions, alike in both strains. Two analogues, 7-deazaadenosine 3',5'-monophosphate (i.e. tubercidin 3',5'-monophosphate) and (RJadenosine 3',5'-monothionophosphate, exhibit higher biological activity than CAMP. The latter analogue is 50-fold more active in both strains. Three analogues showed activities comparable to CAMP, four analogues were less active and 12 analogues were unable to antagonize catabolite repression. Structure-activity correlations showed that the 2'OH-, 3'0-, 5'0-, the negative charge and the 6-amino group cannot be modified without losing biological activity in uivo, while the N-1 and N-7 in adenine are not essential. The interaction with the catabolite gene activator protein is stereoselective for an unmodified axial exocyclic oxygen The molecular mechanism of CAMP action on stimulation of transcription of catabolite-sensitive gene operons was elucidated : a specific cAMP binding protein was isolated and purified. It was named 'catabolite gene activator protein' (CAP) [7] or, alternatively, 'CAMP receptor protein' (CRP) [8]. Regulation by CAP is exerted at the transcriptional level with cAMP acting as an allosteric effector [7,8]. cAMP forms a complex with CAP, thus inducing a conformational change [9], which results in specific recognition of DNA sequences near the promoter of several operons such as lac [lo], gal [ll], araC [12], and increases the rate of transcription initiation. In the lactose [lo] and arabinose operons [12] the CAMP-CAP complex functions as a positive regulator -it potentiates transcription. In the galactose operon, which has two overlapping promoters for RNA polymerase, the complex is required Dedicated to Prof. Dr Friedrich Cramer on the occasion of his 60th birthday.

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On the specificity of cyclic AMP action in Escherichia coli

Cited by 2 publications

References 9 publications

Cyclic AMP Directly Activates NasP, an N -Acyl Amino Acid Antibiotic Biosynthetic Enzyme Cloned from an Uncultured β-Proteobacterium

Cyclic AMP Directly Activates NasP, an N -Acyl Amino Acid Antibiotic Biosynthetic Enzyme Cloned from an Uncultured β-Proteobacterium

Investigations on stimulation of lac transcription in vivo in Escherichia coli by cAMP analogues

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