Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 428, Issue 6, Pages 1197-1208Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2016.02.007
Keywords
PRMT; oligomerization; X-ray crystallography; small angle X-ray scattering; FRET
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Funding
- Japanese Ministry of Education, Culture, Sports, Science, and Technology, Japan (MEXT)
- JSPS Japanese German Graduate Externship
- Senri-Life Science Foundation
- Takeda Science Foundation
- Open Innovation Core (OIC) project of Life Science Center, Tsukuba Advanced Research Alliance, University of Tsukuba, Japan
- MEXT
- Platform Project for Supporting in Drug Discovery and Life Science Research from MEXT
- Japan Agency for Medical Research and Development (AMED)
- Cooperative Research Program of Institute for Protein Research, Osaka University [2012 A6729, 2012B6729, 2013 A6832, 2013B6832, 2014 A6933, 2014B6933]
- Grants-in-Aid for Scientific Research [15K14707, 25252062] Funding Source: KAKEN
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Protein arginine methyltransferase 8 (PRMT8) is unique among PRMTs, as it is specifically expressed in brain and localized to the plasma membrane via N-terminal myristoylation. Here, we describe the crystal structure of human PRMT8 (hPRMT8) at 3.0-angstrom resolution. The crystal structure of hPRMT8 exhibited a novel helical assembly. Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution. This octameric structure is necessary for proper localization to the plasma membrane and efficient methyltransferase activity. The helical assembly might be a relevant quaternary form for hPRMT1, which is the predominant PRMT in mammalian cells and most closely related to hPRMT8. (C) 2016 Elsevier Ltd. All rights reserved.
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