Reactome | PRMT5 can methylate histone H4 at arginine-4 (H4R3)and histo...

Schema > Summation > Entries

created	[InstanceEdit:5205870] Jupe, S, 2013-12-06
dbId	5205838
displayName	PRMT5 can methylate histone H4 at arginine-4 (H4R3)and histo...
literatureReference	[LiteratureReference:3215351] Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes [LiteratureReference:5212680] The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5 [LiteratureReference:5211309] PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing
modified	[InstanceEdit:5216237] Jupe, S, 2013-12-16
schemaClass	Summation
text	PRMT5 can methylate histone H4 at arginine-4 (H4R3)and histone H2A at arginine-4 (H2AR3) (Pal et al. 2004). Symmetric dimethylation of histone H4 arginine-4 (H4R3me2s) by PRMT5 is required for subsequent DNA methylation. The histone-binding protein Cooperator of PRMT5 (COPRS) guides PRMT5:WDR77 to methylate histone H4 arginine-4 (H4R3) rather than histone H3 arginine-9 (H3R8) (Lacroix et al. 2008). H4R3me2s serves as a direct binding target for the DNA methyltransferase DNMT3A, which interacts through the ADD domain, which contains a PHD motif (Zhao et al. 2009).

(summation)

Cite Us!