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