Histone H2A and H4 N-terminal Tails Are Positioned by the MEP50 WD Repeat Protein for Efficient Methylation by the PRMT5 Arginine Methyltransferase

The protein arginine methyltransferase PRMT5 is complexed with the WD repeat protein MEP50 (also known as Wdr77 or androgen coactivator p44) in vertebrates in a tetramer of heterodimers. MEP50 is hypothesized to be required for protein substrate recruitment to the catalytic domain of PRMT5. Here we...

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Библиографические подробности
Опубликовано в: :J Biol Chem
Главные авторы: Burgos, Emmanuel S., Wilczek, Carola, Onikubo, Takashi, Bonanno, Jeffrey B., Jansong, Janina, Reimer, Ulf, Shechter, David
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Biochemistry and Molecular Biology 2015
Предметы:
Enzymology
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC4392268/
https://ncbi.nlm.nih.gov/pubmed/25713080
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M115.636894
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