Disease relevance of PRMT7

• Examination of PRMT7 expressed in E. coli demonstrated that peptides corresponding to sequences contained in histone H4, myelin basic protein, and SmD3 were methylated [1].

High impact information on PRMT7

• The data demonstrate that PRMT7 (like PRMT5) is a Type II methyltransferase capable of producing SDMA modifications in proteins [1].
• PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine [1].
• Immunopurified PRMT7 actively methylated histones, myelin basic protein, a fragment of human fibrillarin (GAR) and spliceosomal protein SmB [1].
• We have identified a mammalian arginine N-methyltransferase, PRMT7, that can catalyze the formation of omega-NG-monomethylarginine in peptides [2].
• An additional unique feature of PRMT7 is that it seems to have arisen from a gene duplication event and contains two putative AdoMet-binding motifs [2].

Biological context of PRMT7

• PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity [2].
• These results suggest that CTCFL and PRMT7 may play a role in male germline imprinted gene methylation [3].

Anatomical context of PRMT7

• Symmetrical dimethyl arginine 3 of histone H4, a modification catalyzed by PRMT7, accumulates in germ cells during this developmental period [3].
• PRMT7, a protein arginine methyltransferase with which CTCFL interacts, is also expressed during embryonic testis development [3].

Associations of PRMT7 with chemical compounds

• The Testis-Specific Factor CTCFL Cooperates with the Protein Methyltransferase PRMT7 in H19 Imprinting Control Region Methylation [3].

Regulatory relationships of PRMT7

• In vitro studies demonstrate that CTCFL stimulates the histone-methyltransferase activity of PRMT7 via interactions with both histones and PRMT7 [3].

Other interactions of PRMT7

• GST fusions of PRMT4 or PRMT7 were unable to methylate the full-length protein or its degradation products [4].

References