Structural and functional relationships between Pasteurella multocida and enterobacterial adenylate cyclases

Mock, Michèle; Crasnier, Martine; Duflot, Edith; Dumay, Valérie; Danchin, Antoine

doi:10.1128/jb.173.19.6265-6269.1991

Cited by 19 publications

(7 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Interestingly, introduction of the Pasteurella multocida cya gene in an E. coli crp strain also leads to an increased level of cAMP synthesis compared with the crp crr double mutant. Perhaps a similar IIAGladenylate cyclase interaction is present in P. multocida (297).…”

Section: Inducer Exclusionmentioning

confidence: 86%

Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.

Postma

Lengeler

Jacobson

1993

Microbiological Reviews

1,028

719

View full text Add to dashboard Cite

MTP' R. capsulatus 86,360 542 (S) a Proteins that have been purified to homogeneity and/or for which a complete or partial gene sequence is known. b Numbers in boldface type are precise molecular weights calculated from the determined or deduced amino acid sequence. Other Mrs are estimates of the monomer molecular weight from denaturing gel electrophoresis. Els for which there is good evidence that the native protein is a homodimer are indicated. c Abbreviations: P, references for purification of the protein; S, references for the complete sequence of the gene or protein; s, references for only a partial sequence; c, molecular weight determined by the size of the product expressed from the cloned gene.

show abstract

Section: Inducer Exclusionmentioning

confidence: 86%

Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.

Postma

Lengeler

Jacobson

1993

Microbiological Reviews

1,028

719

View full text Add to dashboard Cite

show abstract

“…In H. influenzae, the presence of a PTS has not been demonstrated. However, both the putative catalytic and regulatory domains of the H. influenzae adenylate cyclase are homologous to those of the P. multocida enzyme, which has been shown to be subject to PTS regulation in E. coli (25). Because control of adenylate cyclase is probably a key regulator of competence, we are at present investigating whether H. influenzae has phosphoenol pyruvate-dependent (39) first observed that addition of cAMP only raised transformation frequencies to the level that develops spontaneously at the onset of the stationary phase, which is about 100-fold lower than that seen after transfer of exponentially growing cultures to MIV.…”

Section: Discussionmentioning

confidence: 99%

The Haemophilus influenzae adenylate cyclase gene: cloning, sequence, and essential role in competence

1993

View full text Add to dashboard Cite

Competence for transformation in Haemophilus influenzae is stimulated by cyclic AMP (cAMP) and requires the cAMP-dependent catabolite regulatory protein CRP. Thus, understanding the control of competence will require understanding how cAMP levels are regulated. As a first step, we have cloned the H. influenzae adenylate cyclase gene (cya) by complementing the Lac -phenotype of Acya Escherichia coli. Its sequence specifies an 843-amino-acid protein which has significant identity to other known bacterial adenylate cyclases (41 to 43% and 61% identical to the cya genes of enteric bacteria and of Pasteurella multocida, respectively). As seen in other bacterial cya genes, there is evidence for regulation similar to that demonstrated for E. coli: the presence of a strong consensus CRP binding site within the promoter of the gene may provide feedback control of cAMP levels by repressing cya transcription, and translation may be limited by the weak ribosome binding site and by initiation of protein synthesis with GUG rather than AUG or the UUG used in other bacterial cya genes. We confirmed the essential role of cAMP in competence by constructing and characterizing H. influenzae cya mutants. This strain failed to develop competence either spontaneously or after transfer to a competenceinducing medium. However, it became as competent as its wild-type parent in the presence of exogenous cAMP. This result suggests that the failure of exogenously added cAMP to induce optimum competence in wild-type cells is not due to a limitation to the entry of cAMP into the cells. Rather, it strongly favors models in which competence induction requires both an increase in intracellular cAMP and a second as yet unidentified regulatory event. H. influenzae strains mutant in cya or crp were unable to ferment xylose or ribose. This confirms that H. influenzae, like E. coli, uses cAMP and CRP to regulate nutrient uptake and utilization and lends increasing support to the hypothesis that DNA uptake is a mechanism of nutrient acquisition.Although it is almost 50 years since bacterial transformation revealed that DNA carries genetic information (3), we still know very little about how or why some bacteria are able to take up exogenous DNA. Specifically, we do not know how transformable bacteria decide to become competent, we do not know how DNA is translocated across the cell envelope, and we do not know why these transformation systems ever evolved in the first place. In order to answer the last of these questions, we are investigating the first, guided by the principle that the regulatory mechanisms controlling competence development evolved to maximize its benefits and minimize its costs.DNA uptake could have evolved to provide cells with nutrients, with templates for DNA repair, or with novel genetic

show abstract

“…It has never been reported that a prokaryote possesses so many different kinds of cya. Most bacterial adenylate cyclases have been isolated from members of the enterobacterial family, such as E. coli, which has a single cya gene (1,13,14,33,49). As exceptions, it has been reported that R. meliloti possesses at least three cya genes (3) and that Stigmatella aurantiaca possesses two cya genes (13).…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of multiple adenylate cyclase genes from the cyanobacterium Anabaena sp. strain PCC 7120

Katayama

Ohmori

1997

J Bacteriol

View full text Add to dashboard Cite

Adenylate cyclase genes, designated cyaA, cyaB1, cyaB2, cyaC, and cyaD, were isolated from the filamentous cyanobacterium Anabaena sp. strain PCC 7120 by complementation of a strain of Escherichia coli defective for the presence of cya. These genes encoded polypeptides consisting of 735, 859, 860, 1,155, and 546 amino acid residues, respectively. Deduced amino acid sequences of the regions near the C-terminal ends of these cya genes were similar to those of catalytic domains of eukaryotic adenylate cyclases. The remaining part of each cya gene towards its N-terminal end showed a characteristic structure. CyaA had two putative membrane-spanning regions. Both CyaB1 and CyaB2 had regions that were very similar to the cyclic GMP (cGMP)-binding domain of cGMP-stimulated cGMP phosphodiesterase. CyaC consisted of four distinct domains forming sequentially from the N terminus: a response regulator-like domain, a histidine kinase-like domain, a response regulatorlike domain, and the catalytic domain of adenylate cyclase. CyaD contained the forkhead-associated domain in its N-terminal region. Expression of these genes was examined by reverse transcription-PCR. The transcript of cyaC was shown to be predominant in this cyanobacterium. The cellular cyclic AMP level in the disruptant of the cyaC mutant was much lower than that in the wild type.Cyclic AMP (cAMP) regulates various biological activities in both prokaryotes and eukaryotes. In prokaryotes, cAMP and cAMP receptor protein regulate gene expression (7). In eukaryotes, cAMP regulates enzyme activity (11), channel activity (42), and gene expression (34) via the cAMP-dependent protein kinase. In cyanobacteria, it has been reported that cellular cAMP content is affected by growth conditions (17,22), that cAMP concentration changes rapidly in response to light-off and light-on signals (37) or to a pH shift (36), and that cAMP interferes with the pattern formation of heterocysts (43). However, it is still unknown whether cAMP functions as an intracellular signal molecule in cyanobacteria.Recently, we isolated adenylate cyclase (cya) genes from the filamentous cyanobacteria Anabaena cylindrica (26) and Spirulina platensis (52). Regions near the C-terminal ends of the adenylate cyclases of both cyanobacteria showed significant structural similarity to the catalytic domain of the adenylate cyclase of eukaryotes but showed no homology to that of prokaryotes such as Escherichia coli. Furthermore, cyanobacterial adenylate cyclases appeared to be membrane oriented.To study the physiological functions of these adenylate cyclases, disruption or overexpression of cya genes is indispensable. Unfortunately, both A. cylindrica and S. platensis are not transformable, so they are not suitable for this purpose. In this study, we isolated cya genes from a transformable cyanobacterium, Anabaena sp. strain PCC 7120, and constructed mutants defective in cya genes. Some physiological properties of these mutants were determined. MATERIALS AND METHODSStrains and growth conditions. Anabaena sp. s...

show abstract

Structural and functional relationships between Pasteurella multocida and enterobacterial adenylate cyclases

Cited by 19 publications

References 23 publications

Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.

Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.

The Haemophilus influenzae adenylate cyclase gene: cloning, sequence, and essential role in competence

Isolation and characterization of multiple adenylate cyclase genes from the cyanobacterium Anabaena sp. strain PCC 7120

Contact Info

Product

Resources

About