Differential binding of cyclic adenosine 3' ,5'-monophosphate to the cyclic adenosine 3' ,5'-monophosphate receptor protein in Escherichia coli

Danley, Dennis E.; Drexler, Mark; Botsford, James L.

doi:10.1128/jb.130.1.563-565.1977

Cited by 9 publications

(2 citation statements)

References 13 publications

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“…The factor was not found in extracts of cells grown with succinate. This factor does not appear to mediate catabolite repression, at least of tryptophanase induction, as the factor was not found in cell extracts of cells induced for tryptophanase and growing with succinate after the addition of glucose (43).…”

Section: Cyclic Nucleoti'des In Escherichia Coli and Salmonella Typhimentioning

confidence: 93%

Cyclic nucleotides in procaryotes.

Botsford¹

1981

Microbiological Reviews

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113

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Section: Cyclic Nucleoti'des In Escherichia Coli and Salmonella Typhimentioning

confidence: 93%

Cyclic nucleotides in procaryotes.

Botsford¹

1981

Microbiological Reviews

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113

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“…We also observed in one preparation of minicells grown on LB broth the phenomenon described by Anderson and Pastan (2), namely that the cell-free extract showed no cAMP binding activity on day 1 of the experiment but recovered the activity after 3 days at 4°C. These authors, as well as Danley et al (5), pointed out that factors in addition to CAP may mediate the role of cAMP in catabolite repression. We did not see this behavior in any of our other cell extracts, including several LB-grown parent and minicell preparations.…”

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Intracellular location of catabolite activator protein of Escherichia coli

Cook¹,

Revzin²

1980

J Bacteriol

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The catabolite activator protein was assayed in extracts from the minicellproducing Escherichia coli strain P678-54. The level of catabolite activator protein was found to be the same in both parent cells and purified minicells, regardless of whether the bacteria were grown on glucose (which leads to low intracellular cyclic adenosine monophosphate levels) or on glycerol-yeast extract or LB broth (which lead to high cyclic adenosine monophosphate concentrations in the cell). Thus, at any given time most catabolite activator protein molecules are found in the cytoplasm. The implications of this for the mechanism of catabolite activator protein action at catabolite-sensitive operons are discussed.The phenomenon of catabolite repression, in which the synthesis of certain inducible enzymes is inhibited when cells are grown in the presence of glucose, is mediated in Escherichia coli by cyclic AMP (cAMP) and by the catabolite activator protein (CAP), which is also known as the cAMP receptor protein or the catabolite gene activator protein (14,18). A variety of genetic and biochemical data imply that the cAMP-CAP complex is a positive effector of transcription, which stimulates the initiation of mRNA synthesis by RNA polymerase at "catabolitesensitive" operons (6,8,25). In vitro studies have shown that in the absence of cAMP, initiation of transcription at such operons is quite inefficient (6). This correlates with the in vivo data since cAMP levels are relatively low in glucosegrown cells (9,19). A working model for the mechanism of cAMP-CAP action involves its binding to DNA at the promoter region and somehow enhancing the opening of the double helix downstream so that RNA polymerase can melt in to form a stable initiation complex (7,18). CAP will interact with DNA in the absence of cAMP, although the binding affinity is heightened by the cyclic nucleotide (17,23). Specific binding to catabolite-sensitive promoters has been difficult to show in vitro, but has recently been demonstrated (15).To elucidate the molecular details of CAP action we have been quantifying the association of CAP with DNA. We showed that in the absence of cAMP the binding of CAP to nonspecific DNA (which contains no functional CAP sites) is cooperative; that is, the protein is found in clusters on the DNA molecules (23). Addition of cAMP eliminated the cooperativity while increasing the overall affinity of the protein for DNA. We measured association constants for the CAP-DNA interaction at various ionic strengths. The results were extrapolated to presumed physiological ionic conditions to give an estimate of the in vivo binding constant. This value was combined with data for the volume of the bacterial cell and amounts of DNA and of CAP in the cell in a theoretical analysis which predicts the fraction of CAP molecules which should be bound to the chromosome at any given time. The calculation implies that nonspecific binding of CAP to DNA might occur in vivo, perhaps even at low cAMP levels (23). This theoretical approach, when applied to the la...

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cAMP and Regulation of Carbohydrate Metabolism

Botsford

1981

Trends in the Biology of Fermentations for Fuels and Chemicals

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Differential binding of cyclic adenosine 3' ,5'-monophosphate to the cyclic adenosine 3' ,5'-monophosphate receptor protein in Escherichia coli

Cited by 9 publications

References 13 publications

Cyclic nucleotides in procaryotes.

Cyclic nucleotides in procaryotes.

Intracellular location of catabolite activator protein of Escherichia coli

cAMP and Regulation of Carbohydrate Metabolism

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