Cloning and sequencing of the gene encoding the phosphatidylcholine-preferring phospholipase C of Bacillus cereus

Johansen, Terje; Holm, Turid; Guddal, Per Henrik; Sletten, Knut; Haugli, Finn; Little, C. H. A.

doi:10.1016/0378-1119(88)90466-0

Cited by 98 publications

(52 citation statements)

References 39 publications

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“…The enzyme is probably synthesized as a larger precursor before being secreted across the bacterial membrane. Similar results have been reported for the two other secreted B. cereus PLCs (16,35). …”

Section: Discussionsupporting

confidence: 89%

“…Johansen et al (16) and Yamada et al (35) have raised the question whether these three enzymes might be synthesized as one transcriptional unit. Their work has demonstrated that the genes coding for the phosphatidylcholine (PC)-preferring phospholipase C (PLC) and the sphingomyelinase (SM-PLC) reside on contiguous stretches of the B. cereus chromosome, with the PC-PLC gene terminating only about 75 nucleotides upstream from the first coding sequences of the SM-PLC.…”

Section: Discussionmentioning

confidence: 99%

“…To address this question, we translated the entire 2,017-nucleotide stretch of DNA presented in Fig. 1 in all three reading frames and compared these "hypothetical" peptide sequences with the data presented by Johansen et al (16) and Yamada et al (35). No significant homologies to the 5'-flanking region of the PI-PLC gene or the 3'-flanking region of the SM-PLC gene were detected in the alignments of these sequences.…”

Section: Discussionmentioning

confidence: 99%

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Phosphatidylinositol-specific phospholipase C of Bacillus cereus: cloning, sequencing, and relationship to other phospholipases

et al. 1989

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The phosphatidylinositol (PI)-specific phospholipase C (PLC) of Bacillus cereus was cloned into Escherichia coli by using monoclonal antibody probes raised against the purified protein. Phosphoinositide-specific phospholipases C (PLCs) are important enzymes in the regulation of the cellular metabolism of eucaryotic cells. These enzymes have been shown to generate intracellular second messenger molecules in re-

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Section: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Phosphatidylinositol-specific phospholipase C of Bacillus cereus: cloning, sequencing, and relationship to other phospholipases

et al. 1989

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“…The genes that encode PC-PLC and SMase C have recently been cloned and sequenced (2,8,9,30). However, the physiological function of these three exoenzymes has not been established.…”

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confidence: 99%

Apparent phosphate retrieval system in Bacillus cereus

et al. 1989

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Bacillus cereus secretes three different phospholipases C. We studied the effect of P, levels in the growth medium on the production of these exoenzymes. Production of both phosphatidyicholine-preferring phospholipase C and sphingoinyelinase C was repressed by P1 in the growth medium, whereas production of phosphatidylinositol pi&ospholipase C was unaffected. We also found that B. cereus secretes a phsaterepressed alkaline phosphatase activit. Together with a previously reported highly efficient, active uptake system for P,, these three phosphate-repressed exoenzyme activities seem to be part of a phosphate retrieval mechanism that operates under growth-limiting concentrations of Pi. In natural soil systems, which are the natural habitats of B. cereus, the scarcity of P1 is the major growth-limiting factor. A ph reprssed metalloprotease activity was also detected in culture supernatants of B. cereus. It is unclear whether this exoenzyme activity also participates in the proposed phosphate-scavenging system.

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“…4). Recently, a cytolytic determinant of B. cereus GP-4 has been cloned and sequenced and shown to comprise the phospholipase C and sphingomyelinase genes (7,10). The phospholipase C gene was found to be localized on the 1.3-Mb fragment.…”

Section: Resultsmentioning

confidence: 99%