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Calmodulin-like protein from Bacillus subtilis.

I J Fry, L Villa, G D Kuehn

    Biochemical and Biophysical Research Communications
    |January 14, 1986
    PubMed
    Summary
    This summary is machine-generated.

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    Researchers discovered the first calmodulin-like activity in Bacillus subtilis, a Gram-positive bacterium. This calcium-dependent enzyme stimulates cyclic-AMP phosphodiesterase during sporulation.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Molecular Biology

    Background:

    • Calmodulin is a crucial calcium-binding protein regulating cellular processes in eukaryotes.
    • Its presence and function in prokaryotes, particularly Gram-positive bacteria, remain largely unexplored.

    Purpose of the Study:

    • To identify and characterize calmodulin-like activity in the Gram-positive bacterium Bacillus subtilis.
    • To investigate the calcium-dependent regulation of cyclic-AMP phosphodiesterase during bacterial sporulation.

    Main Methods:

    • Analysis of cell-free extracts from Bacillus subtilis undergoing sporulation.
    • Assay of phosphodiesterase-stimulating activity in a calcium-dependent manner.
    • Characterization of the activity's heat stability, binding properties, and inhibition by trifluoperazine.

    Related Experiment Videos

  • Radioimmunoassay to assess cross-reactivity with authentic calmodulin.

    • Main Results:

    • A novel calcium ion-dependent, 3', 5' cyclic-AMP phosphodiesterase-stimulating activity was identified in Bacillus subtilis.
    • The activity demonstrated heat stability and calcium-dependent binding to phenothiazine-agarose, elutable with EGTA.
    • Trifluoperazine reversed the activation, and the activity displaced beef brain calmodulin in radioimmunoassays, indicating calmodulin-like properties.

    Conclusions:

    • This study reports the first evidence of calmodulin-like activity in a Gram-positive bacterium, Bacillus subtilis.
    • The identified activity plays a role in regulating cyclic-AMP phosphodiesterase during sporulation in response to calcium ions.
    • These findings expand our understanding of calcium signaling mechanisms in prokaryotes.