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Related Experiment Videos

Cracking the histone code: one, two, three methyls, you're out!

Robert N Dutnall1

  • 1Section of Molecular Biology, Division of Biological Sciences, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.

Molecular Cell
|July 31, 2003
PubMed
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Nature structural biology·2002

Researchers elucidated the structure of a key enzyme complex involved in histone methylation. This finding offers new ways to understand how different levels of histone methylation regulate gene expression.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Histone methylation is a crucial epigenetic modification regulating gene expression.
  • The SET domain histone methyltransferase DIM-5 plays a role in this process.
  • Understanding the structural basis of methylation is key to deciphering the histone code.

Purpose of the Study:

  • To determine the structure of a ternary complex involving DIM-5.
  • To investigate the role of specific amino acids in histone methylation.
  • To provide insights into the functional significance of histone lysine methylation.

Main Methods:

  • X-ray crystallography was used to determine the structure of the complex.
  • Biochemical assays were performed to analyze enzyme activity.

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  • Structural analysis focused on key amino acid interactions within the complex.

    • Main Results:

    • The ternary complex structure of DIM-5, its cofactor, and a histone H3 peptide was resolved.
    • A key amino acid interaction critical for methyltransferase activity was identified.
    • The structural data provides a foundation for understanding differential histone methylation.

    Conclusions:

    • The determined structure offers a molecular basis for DIM-5 function.
    • This work facilitates the dissection of the functional roles of histone mono-, di-, and trimethylation.
    • The findings contribute to cracking the histone methylation code and understanding epigenetic regulation.