Ligand binding properties of the cytoplasmic cAMP‐binding protein of <i>Dictyostelium discoideum</i>

Wit, René J.W. de; Arents, Jos C.; Driel, Roel van

doi:10.1016/0014-5793(82)81225-8

Cited by 53 publications

(25 citation statements)

References 30 publications

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“…We conclude that the ribose -cyclic phosphate moiety forms hydrogen bonds between its 2', 3' and 5' positions and particular side chains or the backbone of the protein. The same interactions are reported to be essential for binding and subsequent activation of several CAMP-dependent protein kinases [35 -381 and for binding to an intracellular CAMPspecific protein in Dictyostelium discoideum [49]. The chemoreceptor of Dictyostelium forms an essential interaction with only the 3' oxygen [45,61].…”

Section: Structure-activity Correlations and Comparisonmentioning

confidence: 78%

“…Since the R, isomer is much more active than the S, isomer, we deduce an essential ionic interaction of CAP with the axial exocyclic oxygen atom. By contrast, in protein kinases [35 -371 and the intracellular Dictyostelium binding protein [49], the ionic interaction is formed with the equatorial oxygen atom. The proposed stereoselectivity of E. coli for an unmodified axial exocyclic oxygen atom is supported by the results we have obtained with the 5'-amino derivatives of CAMPS (21,22).…”

Section: Structure-activity Correlations and Comparisonmentioning

confidence: 99%

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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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Section: Structure-activity Correlations and Comparisonmentioning

confidence: 78%

Section: Structure-activity Correlations and Comparisonmentioning

confidence: 99%

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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“…discoideum membranes was half-maximal at 3 PM CAMP and reached a maximum of 65% stimulation ( fig.3) [35], which is quite different from the binding specificity of CAMPdependent protein kinase [36], indicating a functional coupling between the cell-surface CAMP receptor and a high-affinity GTPase.…”

Section: Agonist Stimulation Of Gtpase Activitymentioning

confidence: 99%

Agonist‐stimulated high‐affinity GTPase in Dictyostelium membranes

Snaar-Jagalska¹,

Jakobs

Haastert³

1988

FEBS Letters

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“…However, whether the CAMP-dependent kinase, present in D. discoideum [22], is responsible for this phosphorylation in vivo remains to be seen.…”

Section: Discussionmentioning

confidence: 99%

“…CAMP-dependent protein kinase is activated by cIMP and CAMP equally well [21]. The chemotactic receptor binds CAMP about lOOO-fold better than cIMP [22]. The incubation was chilled to 0°C and centrifuged for 2 min at 10000 x g in a microfuge at 4°C.…”

Section: Extracellularmentioning

confidence: 99%

Modulation of the interaction between chemotactic cAMP‐receptor and N‐protein by cAMP‐dependent kinase in Dictyosteliumdiscoideum membranes

1986

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Dictyostelium discoideum cells contain kinetically distinguishable surface CAMP receptors. Both GTP and GDP lower the receptor affinity by inducing conversion of slowly dissociating sites to fast dissociating sites, presumably by binding to a N-protein [(1985) Mol. Cell. B&hem. 67, 119-124, and (1986) Biochemistry 25, 1314. In this paper we show that treatment of isolated membranes with CAMP-dependent protein kinase abolished the GTP-induced receptor transition, but not the one induced by GDP. The effect of GTP on the receptor kinetics could be restored by treatment of the membranes with alkaline phosphatase. These results indicate that in D. discoideum membranes phosphorylation of a signal-transduction component reversibly abolishes the interaction of the CAMP receptor with the NGTP complex, but not that with the NGDP complex.(Dictyostelium discoideum)cyclic AMP receptor N-protein cyclic AMP dependence Protein kinase Desensitization Adaptation

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Ligand binding properties of the cytoplasmic cAMP‐binding protein of Dictyostelium discoideum

Cited by 53 publications

References 30 publications

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

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

Agonist‐stimulated high‐affinity GTPase in Dictyostelium membranes

Modulation of the interaction between chemotactic cAMP‐receptor and N‐protein by cAMP‐dependent kinase in Dictyosteliumdiscoideum membranes

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