Expression, purification, crystallization and preliminary crystallographic study of the SRA domain of the human UHRF1 protein.

Date publication

octobre 2008

Auteurs

Membres identifiés du Cancéropôle Est :
Dr BIRCK Catherine

Tous les auteurs :
Delagoutte B, Lallous N, Birck C, Oudet P, Samama JP

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/18931436

Résumé

Human UHRF1 belongs to the unique mammalian family of proteins which contain a SET- and RING finger-associated (SRA) domain. This 180-residue domain has been reported to play key roles in the functions of the protein. It allows UHRF1 to bind methylated DNA, histone deacetylase 1 and DNA methyltransferase 1, suggesting a bridge between DNA methylation and the histone code. No structural data is available for any SRA domain. Native and SeMet-labelled SRA domains of human UHRF1 were overexpressed in Escherichia coli cells, purified to homogeneity and crystallized using the hanging-drop vapour-diffusion method. A complete MAD data set was collected to 2.2 A resolution at 100 K. Crystals of the SeMet-labelled protein belonged to the trigonal space group P3(2)21, with unit-cell parameters a = b = 53.78, c = 162.05 A.

Référence

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Oct 1;64(Pt