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Elucidation of the function based on the whole structure of rat liver vault, the largest ribonucleo-protein particle 査読

Hideaki Tanaka, Koji Kato, Tomoyuki Sumizawa, Eiki Yamashita

Seikagaku 83 ( 5 ) 392 - 395 2011年

2SJ-05 細胞質内で最大の分子量を持つ核酸-蛋白質複合体ボルトの構造(2SJ タンパク質複合体研究の新展開:分子から超分子、凝集体まで,日本生物物理学会第49回年会(2011年度))

田中秀明, Kato Koji, Yamashita Eiki, Sumizawa Tomoyuki, Zhou Yong, Yao Min, Iwasaki Kenji, Yoshimura Masato, Tsukihara Tomitake

生物物理 51 S23 2011年

ラット肝由来の巨大なRNAタンパク質複合体vaultのX線結晶構造

住澤知之, 加藤公児, 田中秀明

J UOEH Univ Occup Environ Health 32 ( 1 ) 113 2010年3月

25.ラット肝由来の巨大なRNAタンパク質複合体vaultのX線結晶構造(第27回産業医科大学学会総会学術講演会記録)

住澤知之, 加藤公児, 田中秀明

産業医科大学雑誌 32 ( 1 ) 2010年3月

分子量が1000万にも及ぶ生体内巨大分子に対する構造解析

山下栄樹, 加藤公児, 田中秀明

放射光 22 ( 6 ) 284 - 291 2009年11月

ラット肝臓由来ボルトの3.5Å分解能での構造解析招待

加藤公児, 田中秀明, 月原冨武

2009年10月

[X-ray structure of vault: the largest ribonucleoprotein complex]. 査読

Kato K, Tanaka H

Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme 54 1159 - 1165 2009年7月

分子量約1000万の巨大粒子 vault のX線結晶構造解析

田中秀明, 加藤公児, 山下栄樹

日本結晶学会誌 51 ( 3 ) 189 - 194 2009年6月

記述言語：日本語出版者・発行元：日本結晶学会

Vaults are among the largest cytoplasmic ribonucleoprotein particles and are found in numerous eukaryotic species. Although roles in multidrug resistance and innate immunity have been suggested, the cellular function remains unclear. We have determined the X-ray structure of rat liver vault at 3.5 Å resolution. A vault particle shell was composed of 78 MVP (Major vault protein) chains with 39-fold dihedral symmetry. The shoulder domain of MVP is structurally similar to SPFH (stomatin/prohibitin/flotillin/HflK/C) domain involved in lipid raft association.

DOI： 10.5940/jcrsj.51.189

CiNii Article

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X-ray crystal structural determination of rat vault, a large nucleoprotein complex at 3.5Å resolution. 招待

H. Tanaka, K. Kato, E. Yamashita, T. Sumizawa, Y. Zhou, M. Yao, K. Iwasaki, M. Yoshimura, T. Tsukihara

2009年3月

The Structure of Rat Liver Vault at 3.5 Angstrom Resolution 査読

Hideaki Tanaka, Koji Kato, Eiki Yamashita, Tomoyuki Sumizawa, Yong Zhou, Min Yao, Kenji Iwasaki, Masato Yoshimura, Tomitake Tsukihara

SCIENCE 323 ( 5912 ) 384 - 388 2009年1月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：AMER ASSOC ADVANCEMENT SCIENCE

Vaults are among the largest cytoplasmic ribonucleoprotein particles and are found in numerous eukaryotic species. Roles in multidrug resistance and innate immunity have been suggested, but the cellular function remains unclear. We have determined the x-ray structure of rat liver vault at 3.5 angstrom resolution and show that the cage structure consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains. Each MVP monomer folds into 12 domains: nine structural repeat domains, a shoulder domain, a cap-helix domain, and a cap-ring domain. Interactions between the 42-turn-long cap-helix domains are key to stabilizing the particle. The shoulder domain is structurally similar to a core domain of stomatin, a lipid-raft component in erythrocytes and epithelial cells.

DOI： 10.1126/science.1164975

The Structure of Rat Liver Vault at 3.5 Angstrom Resolution 査読

Hideaki Tanaka, Koji Kato, Eiki Yamashita, Tomoyuki Sumizawa, Yong Zhou, Min Yao, Kenji Iwasaki, Masato Yoshimura, Tomitake Tsukihara

Science 49 ( Supplement 1 ) 2009年1月

Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas reuoluta) seeds 査読

Seiya Yokoyama, Kouji Kato, Atsuko Koba, Yuji Minami, Keiichi Watanabec, Fumio Yagi

PEPTIDES 29 ( 12 ) 2110 - 2117 2008年12月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：ELSEVIER SCIENCE INC

Novel antimicrobial peptides (AMP), designated Cy-AMP1, Cy-AMP2, and Cy-AMP3, were purified from seeds of the cycad (Cycas revoluta) by a CM cellulofine column, ion-exchange HPLC on SP COSMOGEL, and reverse-phase HPLC. They had molecular masses of 4583.2 Da, 4568.9 Da and 9275.8 Da, respectively, by MALDI-TOF MS analysis. Half of the amino acid residues of Cy-AMP1 and Cy-AMP2 were cysteine, glycine and proline, and their sequences were similar. The sequence of Cy-AMP3 showed high homology to various lipid transfer proteins. For Cy-AMP1 and Cy-AMP2, the concentrations of peptides required for 50% inhibition (IC(50)) of the growth of plant pathogenic fungi, Gram-positive and Gram-negative bacteria were 7.0-8.9 mu g/ml. The Cy-AMP3 had weak antimicrobial activity. The structural and antimicrobial characteristics of Cy-AMP1 and Cy-AMP2 indicated that they are a novel type of antimicrobial peptide belonging to a plant defensin family. (c) 2008 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.peptides.2008.08.007

Web of Science

PubMed

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X-ray structure of the vault purified from rat liver 招待

田中秀明, 加藤公児, 住澤知之, 山下栄樹, 吉村政人, 周勇, 姚閔, 岩崎憲治, 月原冨武

2008年12月

A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry 査読

Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, Masato Yoshimura, Eiki Yamashita, Kenji Iwasaki, Tomitake Tsukihara

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 64 525 - 531 2008年5月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：BLACKWELL PUBLISHING

Vault is a 12.9 MDa ribonucleoprotein particle with a barrel-like shape, two protruding caps and an invaginated waist structure that is highly conserved in a wide variety of eukaryotes. Multimerization of the major vault protein (MVP) is sufficient to assemble the entire exterior shell of the barrel-shaped vault particle. Multiple copies of two additional proteins, vault poly(ADP-ribose) polymerase (VPARP) and telomerase-associated protein 1 (TEP1), as well as a small vault RNA (vRNA), are also associated with vault. Here, the crystallization of vault particles is reported. The crystals belong to space group C2, with unit-cell parameters a = 708.0, b = 385.0, c = 602.9 angstrom, beta = 124.8 degrees. Rotational symmetry searches based on the R factor and correlation coefficient from noncrystallographic symmetry (NCS) averaging indicated that the particle has 39-fold dihedral symmetry.

DOI： 10.1107/S0907444908004277

Web of Science

PubMed

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1P-002 ラット肝臓由来vaultのX線結晶構造(蛋白質・構造(1),日本生物物理学会若手奨励賞選考会,若手招待講演,第46回日本生物物理学会年会)

Tanaka Hideaki, Kato Koji, Sumizawa Tomoyuki, Yamashita Eiki, Yoshimura Masato, Yong Zhou, Yao Min, Iwasaki Kenji, Tsukihara Tomitake

生物物理 48 S21 2008年

2P041 X-ray crystal structural analysis of vault from rat liver(29. Protein structure and dynamics (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

TANAKA Hideaki, KATO Koji, Yamashita Eiki, FUJITA Chizuko, SUMIZAWA Tomoyuki, TSUKIHARA Tomitake

生物物理 46 ( 2 ) S306 2006年

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