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Cloning, expression, purification and crystallization of Schizosaccharomyces pombe Set7, a putative histone methyltransferase
Author(s) -
Mevius Damiaan E. H. F.,
Shen Yunpeng,
Morishita Masayo,
di Luccio Eric
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16003794
Subject(s) - schizosaccharomyces pombe , histone methyltransferase , histone h2a , histone methylation , histone code , histone h1 , methyltransferase , biology , chromatin , histone , cloning (programming) , genetics , biochemistry , microbiology and biotechnology , nucleosome , yeast , methylation , dna , dna methylation , saccharomyces cerevisiae , gene expression , gene , computer science , programming language
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.