| RRC ID |
36129
|
| Author |
Mevius DE, Shen Y, Morishita M, di Luccio E.
|
| Title |
Cloning, expression, purification and crystallization of Schizosaccharomyces pombe Set7, a putative histone methyltransferase.
|
| Journal |
Acta Crystallogr F Struct Biol Commun
|
| 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.
|
| Volume |
72(Pt 4)
|
| Pages |
263-8
|
| Published |
2016-4-1
|
| DOI |
10.1107/S2053230X16003794
|
| PII |
S2053230X16003794
|
| PMID |
27050258
|
| PMC |
PMC4822981
|
| MeSH |
Amino Acid Sequence
Base Sequence
Cloning, Molecular
Crystallization
Histone Methyltransferases
Histone-Lysine N-Methyltransferase
Schizosaccharomyces / chemistry*
Schizosaccharomyces pombe Proteins / chemistry
Schizosaccharomyces pombe Proteins / genetics*
Schizosaccharomyces pombe Proteins / isolation & purification*
|
| IF |
0.968
|
| Times Cited |
1
|
|
WOS Category
|
BIOCHEMICAL RESEARCH METHODS
BIOCHEMISTRY & MOLECULAR BIOLOGY
BIOPHYSICS
CRYSTALLOGRAPHY
|
| Resource |
| Yeast |
cDNA library |
