Novel helical assembly in arginine methyltransferase 8

Sachiko Toma-Fukai; Jun Dal Kim; Kyung Eui Park; Naoyuki Kuwabara; Nobutaka Shimizu; Elena Krayukhina; Susumu Uchiyama; Akiyoshi Fukamizu; Toshiyuki Shimizu

doi:10.1016/j.jmb.2016.02.007

Novel helical assembly in arginine methyltransferase 8

Sachiko Toma-Fukai, Jun Dal Kim, Kyung Eui Park, Naoyuki Kuwabara, Nobutaka Shimizu, Elena Krayukhina, Susumu Uchiyama, Akiyoshi Fukamizu, Toshiyuki Shimizu^*

^*Corresponding author for this work

Complex Biosystem Research, Institute of Natural Medicine

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

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-Å 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.

Original language	English
Pages (from-to)	1197-1208
Number of pages	12
Journal	Journal of Molecular Biology
Volume	428
Issue number	6
DOIs	https://doi.org/10.1016/j.jmb.2016.02.007
State	Published - 2016/03/27

Keywords

FRET
PRMT
X-ray crystallography
oligomerization
small angle X-ray scattering

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.jmb.2016.02.007

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title = "Novel helical assembly in arginine methyltransferase 8",

abstract = "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-{\AA} 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.",

keywords = "FRET, PRMT, X-ray crystallography, oligomerization, small angle X-ray scattering",

author = "Sachiko Toma-Fukai and Kim, {Jun Dal} and Park, {Kyung Eui} and Naoyuki Kuwabara and Nobutaka Shimizu and Elena Krayukhina and Susumu Uchiyama and Akiyoshi Fukamizu and Toshiyuki Shimizu",

year = "2016",

month = mar,

day = "27",

doi = "10.1016/j.jmb.2016.02.007",

language = "英語",

volume = "428",

pages = "1197--1208",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "6",

}

TY - JOUR

T1 - Novel helical assembly in arginine methyltransferase 8

AU - Toma-Fukai, Sachiko

AU - Kim, Jun Dal

AU - Park, Kyung Eui

AU - Kuwabara, Naoyuki

AU - Shimizu, Nobutaka

AU - Krayukhina, Elena

AU - Uchiyama, Susumu

AU - Fukamizu, Akiyoshi

AU - Shimizu, Toshiyuki

PY - 2016/3/27

Y1 - 2016/3/27

N2 - 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-Å 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.

AB - 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-Å 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.

KW - FRET

KW - PRMT

KW - X-ray crystallography

KW - oligomerization

KW - small angle X-ray scattering

UR - http://www.scopus.com/inward/record.url?scp=84962044982&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2016.02.007

DO - 10.1016/j.jmb.2016.02.007

M3 - 学術論文

C2 - 26876602

AN - SCOPUS:84962044982

SN - 0022-2836

VL - 428

SP - 1197

EP - 1208

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 6

ER -

Novel helical assembly in arginine methyltransferase 8

Abstract

Keywords

ASJC Scopus subject areas

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