콘텐츠로 건너뛰기
Merck
  • PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine.

PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine.

The Journal of biological chemistry (2004-10-21)
Jin-Hyung Lee, Jeffry R Cook, Zhi-Hong Yang, Olga Mirochnitchenko, Samuel I Gunderson, Arthur M Felix, Nicole Herth, Ralf Hoffmann, Sidney Pestka
초록

The cDNA for PRMT7, a recently discovered human protein-arginine methyltransferase (PRMT), was cloned and expressed in Escherichia coli and mammalian cells. Immunopurified PRMT7 actively methylated histones, myelin basic protein, a fragment of human fibrillarin (GAR) and spliceosomal protein SmB. Amino acid analysis showed that the modifications produced were predominantly monomethylarginine and symmetric dimethylarginine (SDMA). Examination of PRMT7 expressed in E. coli demonstrated that peptides corresponding to sequences contained in histone H4, myelin basic protein, and SmD3 were methylated. Furthermore, analysis of the methylated proteins showed that symmetric dimethylarginine and relatively small amounts of monomethylarginine and asymmetric dimethylarginine were produced. SDMA was also formed when a GRG tripeptide was methylated by PRMT7, indicating that a GRG motif is by itself sufficient for symmetric dimethylation to occur. Symmetric dimethylation is reduced dramatically compared with monomethylation as the concentration of the substrate is increased. The data demonstrate that PRMT7 (like PRMT5) is a Type II methyltransferase capable of producing SDMA modifications in proteins.

MATERIALS
제품 번호
브랜드
제품 설명

Sigma-Aldrich
PRMT7 human, recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)