research communications
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.
Keywords: histone modifications; histone methyltransferase; Schizosaccharomyces pombe; Set7; X-ray crystallography.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S2053230X16003794/nw5035sup1.pdf |