Unknown

Dataset Information

0

Cloning, expression, purification and crystallization of Schizosaccharomyces pombe Set7, a putative histone methyltransferase.


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.

SUBMITTER: Mevius DE 

PROVIDER: S-EPMC4822981 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cloning, expression, purification and crystallization of Schizosaccharomyces pombe Set7, a putative histone methyltransferase.

Mevius Damiaan E H F DE   Shen Yunpeng Y   Morishita Masayo M   di Luccio Eric E  

Acta crystallographica. Section F, Structural biology communications 20160316 Pt 4


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-  ...[more]

Similar Datasets

| S-EPMC3605359 | biostudies-literature
| S-EPMC1151661 | biostudies-literature
| S-EPMC3976068 | biostudies-literature
| S-EPMC115158 | biostudies-literature
| S-EPMC2815687 | biostudies-literature
| S-EPMC4826183 | biostudies-literature
| S-EPMC3433193 | biostudies-literature
| S-EPMC6450525 | biostudies-literature
| S-EPMC3160588 | biostudies-literature
| S-EPMC8024890 | biostudies-literature