Two functional domains in adenylate cyclase of Escherichia coli

Roy, A. K.; Danchin, Antoine; Joseph, Evelyne; Ullmann, Agnès

doi:10.1016/s0022-2836(83)80251-4

Cited by 49 publications

(31 citation statements)

References 12 publications

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“…The former region cannot at present be related to a specific function of the protein, whereas the latter is a region that can be considered a hinge joining the catalytic and the regulatory domains of the protein (20). Another feature of these proteins is the high amount of cysteine and histidine residues.…”

Section: Resultsmentioning

confidence: 99%

“…Different C-terminal truncated forms of E. coli AC have been shown to retain enzymatic activity (20) but have lost the regulation leading to the high production of cAMP in crp strains (4). On the basis of these experiments, it has been proposed that E. coli AC is composed of two functional domains: the amino-terminal catalytic domain and the carboxy-terminal regulatory domain (20), the latter being required for both the glucose effect and the CAP-dependent activation process (4).…”

Section: Resultsmentioning

confidence: 99%

“…On the basis of these experiments, it has been proposed that E. coli AC is composed of two functional domains: the amino-terminal catalytic domain and the carboxy-terminal regulatory domain (20), the latter being required for both the glucose effect and the CAP-dependent activation process (4). In the case of P. multocida AC, both truncated forms were active (as shown by the complementation experiments) but no cAMP excretion was obtained on MacConkey plates with the Acya Acrp strain containing either pPMA140 or pPMA150 carrying truncated genes (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…It has also been shown that the large increase of cAMP synthesis occurring in crp strains (deficient in CAP) (10) is dependent on the presence of enzyme III-glucose (4). In addition, gene deletion experiments have indicated that the carboxy-terminal domain of the protein is required for the regulation of AC activity by enzyme III-glucose (4,20).…”

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confidence: 99%

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Structural and functional relationships between Pasteurella multocida and enterobacterial adenylate cyclases

et al. 1991

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The Pasteurella multocida adenylate cyclase gene has been cloned and expressed in Escherichia coli. The primary structure of the protein (838 amino acids) deduced from the corresponding nucleotide sequence was compared with that of E. coli. The two enzymes have similar molecular sizes and, based on sequence conservation at the protein level, are likely to be organized in two functional domains: the amino-terminal catalytic domain and the carboxy-terminal regulatory domain. 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. This increase does not occur in strains deficient in both the catabolite gene activator protein and enzyme HI-glucose, indicating that a protein similar to E. coli enzyme III-glucose is involved in the regulation ofP. multocida adenylate cyclase. It also indicates that the underlying process leading to enterobacterial adenylate cyclase activation has been conserved through evolution.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Structural and functional relationships between Pasteurella multocida and enterobacterial adenylate cyclases

et al. 1991

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“…Antoine Danchin succeeded in cloning the cya gene and demonstrated that the bacterial adenylate cyclase consisted of two functional domains: an amino-terminal domain exhibiting cyclase catalytic activity and a carboxy-terminal domain having regulatory functions. Antoine then constructed a cya-lacZ fusion that coded for both adenylate cyclase and β-galactosidase activities (39).…”

Section: Escherichia Coli Adenylate Cyclasementioning

confidence: 99%

A Fortunate Journey on Uneven Grounds

Ullmann

2012

Annu. Rev. Microbiol.

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I was surprised to be invited to write a prefatory chapter for the Annual Review of Microbiology. Indeed, I did not feel that I belonged to that class of eminent scientists who had written such chapters. Perhaps it is because I am a kind of mutant: In spite of having experienced war, both German and Soviet occupations, repeated bombardments, dictatorships, and a revolution, I managed nonetheless to engage in scientific research, thus realizing a childhood dream. After having obtained my Doctor Rerum Naturalium degree in Budapest, Hungary, I was fortunate to meet Jacques Monod at the Pasteur Institute, and this became a turning point in my scientific career. In his laboratory, I contributed to the definition of the lactose operon promoter, uncovered intracistronic complementation in β-galactosidase, and investigated the role of cAMP in Escherichia coli. In my own laboratory, together with many gifted students and collaborators, I studied the role of adenylate cyclase in bacterial virulence. This allowed the engineering of recombinant adenylate cyclase toxin from Bordetella pertussis for the development of protective and therapeutic vaccines.

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cAMP Signaling in Prokaryotes

Jahreis

2009

Bacterial Signaling

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Two functional domains in adenylate cyclase of Escherichia coli

Cited by 49 publications

References 12 publications

Structural and functional relationships between Pasteurella multocida and enterobacterial adenylate cyclases

Structural and functional relationships between Pasteurella multocida and enterobacterial adenylate cyclases

A Fortunate Journey on Uneven Grounds

cAMP Signaling in Prokaryotes

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