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Structure and function of DNA methyltransferases

X Cheng1

  • 1W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, New York 11724, USA.

Annual Review of Biophysics and Biomolecular Structure
|January 1, 1995
PubMed
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DNA methylation plays key roles in prokaryotes and eukaryotes. Structural studies reveal a common catalytic domain in S-adenosyl-L-methionine (SAM)-dependent methyltransferases, enabling structure prediction for diverse enzymes.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • DNA methylation in prokaryotes primarily serves as a defense mechanism against restriction enzymes.
  • In eukaryotes, DNA methylation is crucial for cellular differentiation, gene regulation, and embryonic development.
  • S-adenosyl-L-methionine (SAM)-dependent methyltransferases are enzymes involved in various biological processes.

Purpose of the Study:

  • To investigate the structural and enzymatic properties of SAM-dependent DNA-modifying enzymes.
  • To understand the mechanism of nucleotide modification by DNA methyltransferases.
  • To explore the evolutionary conservation of catalytic domains among methyltransferases.

Main Methods:

  • X-ray crystallography was used to determine the structure of HhaI DNA methyltransferase.

Related Experiment Videos

  • Comparative structural analysis of HhaI, TaqI, and catechol O-methyltransferase.
  • Bioinformatic approaches for predicting tertiary structures based on amino acid sequences.

    • Main Results:

    • The HhaI enzyme mechanism involves flipping the substrate nucleotide out of the DNA helix.
    • A conserved catalytic-domain structure was identified across three distinct SAM-dependent methyltransferases.
    • This conserved domain suggests a common evolutionary origin and functional mechanism.

    Conclusions:

    • The structural similarity of methyltransferases allows for prediction of tertiary structures for uncharacterized enzymes.
    • This finding has implications for understanding and potentially engineering a wide range of methyltransferases, including eukaryotic CpG methyltransferases.
    • The study provides insights into the catalytic mechanisms and evolutionary relationships of DNA-modifying enzymes.