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Related Experiment Videos

Structure-based sequence alignment of three AdoMet-dependent DNA methyltransferases

M O'Gara1, K McCloy, T Malone

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

Gene
|May 19, 1995
PubMed
Summary

DNA methyltransferases (MTases) like M.HhaI, M.TaqI, and COMT share similar protein structures. Structural alignment reveals conserved motifs, suggesting a common catalytic domain across many AdoMet-dependent MTases.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • DNA methyltransferases (MTases) are enzymes that transfer methyl groups from S-adenosylmethionine (AdoMet).
  • Key MTases include M.HhaI, M.TaqI, and Catechol-O-methyltransferase (COMT), each with distinct substrates.
  • These enzymes play crucial roles in various biological processes, including DNA modification and gene regulation.

Purpose of the Study:

  • To investigate the structural similarities between M.HhaI, M.TaqI, and COMT.
  • To identify conserved structural motifs within the catalytic domains of these enzymes.
  • To explore the implications for a common catalytic domain structure in AdoMet-dependent MTases.

Main Methods:

  • Comparative structural analysis of the catalytic domains of M.HhaI, M.TaqI, and COMT.

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  • Utilizing structural alignment techniques with backbone modifications (insertions/deletions).
  • Sequence analysis to identify conserved amino acid motifs.

    • Main Results:

    • The catalytic domains of M.HhaI, M.TaqI, and COMT exhibit similar alpha/beta fold structures with a central mixed beta-sheet.
    • Structural alignment revealed conserved motifs, particularly when accounting for backbone variations.
    • Equivalence in amino acid sequences was observed between M.TaqI and COMT.

    Conclusions:

    • M.HhaI, M.TaqI, and COMT share significant structural homology in their catalytic domains.
    • The findings suggest that many AdoMet-dependent methyltransferases may possess a common evolutionary origin and catalytic domain structure.
    • This structural conservation has implications for understanding enzyme function and evolution.