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Calmodulin N-methyltransferase. Partial purification and characterization.

P M Rowe, L S Wright, F L Siegel

    The Journal of Biological Chemistry
    |May 25, 1986
    PubMed
    Summary
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    Rat calmodulin N-methyltransferase is a cytosolic enzyme with high substrate specificity for calmodulin. Its distribution correlates with calmodulin levels, and methylation does not affect calmodulin

    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Biology

    Background:

    • S-adenosylmethionine:calmodulin (lysine) N-methyltransferase (calmodulin N-methyltransferase) is a key enzyme in calmodulin post-translational modification.
    • The enzyme's distribution and substrate specificity are crucial for understanding its biological role.
    • Calmodulin methylation is a poorly understood process with potential functional implications.

    Purpose of the Study:

    • To investigate the distribution, properties, and substrate specificity of rat calmodulin N-methyltransferase.
    • To purify and characterize the enzyme.
    • To explore the functional consequences of calmodulin methylation.

    Main Methods:

    • Enzyme purification using ammonium sulfate precipitation and various chromatography techniques (DEAE-cellulose, CM-Sepharose, Sephadex G-100).

    Related Experiment Videos

  • Enzyme activity assays using [methyl-3H]AdoMet and tissue extracts.
  • In vitro preparative methylation of des(methyl)-calmodulin from Dictyostelium discoideum.
  • Analysis of methylated proteins via electrophoresis.
  • Functional assays measuring cyclic nucleotide phosphodiesterase activation.

    • Main Results:

    • Calmodulin N-methyltransferase is cytosolic and its levels correlate with tissue calmodulin concentrations.
    • The enzyme was purified 470-fold from rat testis cytosol, exhibiting an apparent molecular weight of 55,000.
    • Purified enzyme demonstrated high substrate specificity, exclusively methylating calmodulin.
    • In vitro methylation of des(methyl)-calmodulin incorporated three methyl groups, forming trimethyllysine at lysine 115.
    • Methylation did not alter calmodulin's ability to activate cyclic nucleotide phosphodiesterase.

    Conclusions:

    • Rat calmodulin N-methyltransferase is a specific enzyme involved in calmodulin methylation.
    • The enzyme's distribution suggests a role in regulating calmodulin function based on cellular calmodulin levels.
    • Calmodulin methylation, while occurring specifically, does not appear to affect its primary function in phosphodiesterase activation.