[HTML][HTML] Histone H2A and H4 N-terminal tails are positioned by the MEP50 WD repeat protein for efficient methylation by the PRMT5 arginine methyltransferase
ES Burgos, C Wilczek, T Onikubo, JB Bonanno… - Journal of Biological …, 2015 - ASBMB
Background: PRMT5-MEP50 is an arginine methyltransferase with significant roles in
development and cancer. Results: MEP50 binds to the histone fold domain and is essential
for the efficient use of SAM by PRMT5. Conclusion: MEP50 is essential for methylation of
histones H4 and H2A by PRMT5. Significance: The mechanism of histone methylation by
PRMT5-MEP50 provides novel insight into methyltransferase mechanisms and therapeutic
development. The protein arginine methyltransferase PRMT5 is complexed with the WD …
development and cancer. Results: MEP50 binds to the histone fold domain and is essential
for the efficient use of SAM by PRMT5. Conclusion: MEP50 is essential for methylation of
histones H4 and H2A by PRMT5. Significance: The mechanism of histone methylation by
PRMT5-MEP50 provides novel insight into methyltransferase mechanisms and therapeutic
development. The protein arginine methyltransferase PRMT5 is complexed with the WD …