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Updated: Mar 23, 2026
Genetic Screen for Identification of Multicopy Suppressors in Schizosaccharomyces pombe
Published on: September 13, 2022
Cloning, expression, purification and crystallization of Schizosaccharomyces pombe Set7, a putative histone
Damiaan E H F Mevius1, Yunpeng Shen1, Masayo Morishita1
1Genetic Engineering Department, School of Life Sciences, College of Natural Sciences, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of Korea.
Abstract:
Dysfunction of histone-modifying enzymes affects chromatin regulation and is involved in carcinogenesis, tumour progression and other diseases. Histone methyltransferases are a family of key histone-modifying enzymes, but their structures, functions and mechanisms are incompletely understood, thus constraining drug-design efforts. Here, preliminary steps towards structure-function studies of Schizosaccharomyces pombe Set7, a putative histone methyltransferase and the first yeast full-length SET-domain-containing protein to be studied using X-ray crystallography, are reported. The methods from cloning to X-ray diffraction and phasing are discussed and the results will aid in prospective studies of histone-modifying enzymes.
Insights
This study reports preliminary steps toward understanding histone methyltransferases using X-ray crystallography of yeast Set7. These findings will advance research into chromatin regulation and disease-related enzyme mechanisms.
Area of Science:
- Biochemistry and Molecular Biology
- Structural Biology
- Epigenetics
Background:
- Histone-modifying enzymes are crucial for chromatin regulation and implicated in diseases like cancer.
- Histone methyltransferases, a key class of these enzymes, remain poorly understood regarding their structure and function.
- This lack of understanding hinders the development of targeted drugs for related diseases.
Purpose of the Study:
- To initiate structure-function studies of Schizosaccharomyces pombe Set7, a yeast histone methyltransferase.
- To provide preliminary structural insights into a full-length SET-domain-containing protein from yeast.
- To lay the groundwork for future investigations into histone-modifying enzyme mechanisms.
Main Methods:
- Cloning of the Schizosaccharomyces pombe Set7 gene.
- Expression and purification of the Set7 protein.
- X-ray diffraction data collection, structure determination, and phasing.
Main Results:
- Successful cloning and expression of the yeast Set7 protein.
- Acquisition of X-ray diffraction data enabling structural analysis.
- Preliminary structural insights into a key histone methyltransferase.
Conclusions:
- The study presents initial steps towards the structural and functional characterization of yeast Set7.
- The reported methods and preliminary results facilitate future research on histone methyltransferases.
- This work is expected to aid in understanding enzyme mechanisms and inform drug design efforts.
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