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Sequence-specific BamHI methylase. Purification and characterization.

G Nardone, J George, J G Chirikjian

    The Journal of Biological Chemistry
    |August 25, 1984
    PubMed
    Summary
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    BamHI methylase, purified to homogeneity, functions as a single polypeptide. This enzyme requires S-adenosyl-L-methionine and is inhibited by Mg2+, with roles for arginine and cysteine residues identified.

    Area of Science:

    • Molecular Biology
    • Enzymology

    Background:

    • BamHI methylase is an enzyme involved in DNA modification.
    • Understanding its properties is crucial for molecular biology applications.

    Purpose of the Study:

    • To purify and characterize BamHI methylase.
    • To investigate its mechanism of action and substrate specificity.

    Main Methods:

    • Protein purification using standard biochemical techniques.
    • Enzyme activity assays with S-adenosyl-L-methionine.
    • Inhibition studies using Mg2+, 2,3-butanedione, and N-ethylmaleimide.
    • Electrophoresis for molecular weight determination.

    Main Results:

    • BamHI methylase purified as a single 56,000 MW polypeptide.

    Related Experiment Videos

  • The enzyme requires S-adenosyl-L-methionine and is inhibited by Mg2+.
  • Arginine and cysteine residues are important for activity, with differential protection by DNA and S-adenosyl-L-methionine.
  • Methylation occurs on both DNA strands in a single binding event.
  • Glycerol addition relaxes sequence specificity.

    • Conclusions:

    • BamHI methylase is a monomeric enzyme with distinct properties from its endonuclease counterpart.
    • Key amino acid residues and cofactors are identified.
    • The mechanism involves simultaneous modification of both DNA strands.
    • Reaction conditions can alter enzyme specificity.