Faculty Profiles - KATOU Kouji

Papers - KATOU Kouji

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

Hideaki Tanaka, Koji Kato, Tomoyuki Sumizawa, Eiki Yamashita

Seikagaku 83 ( 5 ) 392 - 395 2011

2SJ-05 X-ray structure of the vault, the largest cytoplasmic ribonucleo protein particle(2SJ New developments in protein complex research: From molecules to supramolecules and aggregates,The 49th Annual Meeting of the Biophysical Society of Japan)

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

Seibutsu Butsuri 51 S23 2011

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 2010.3

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 ) 2010.3

X-ray structure analysis of a 10MDa biological macromolecule

YAMASHITA Eiki, KATO Koji, TANAKA Hideaki

22 ( 6 ) 284 - 291 2009.11

ラット肝臓由来ボルトの3.5Å分解能での構造解析 Invited

加藤公児, 田中秀明, 月原冨武

2009.10

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

Kato K, Tanaka H

Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme 54 1159 - 1165 2009.7

X-ray Crystal Structure of the Vault, Largest Ribonucleoprotein Particle, with a Molecular Weight of 10MDa

TANAKA Hideaki, KATO Koji, YAMASHITA Eiki

Nihon Kessho Gakkaishi 51 ( 3 ) 189 - 194 2009.6

Language：Japanese Publisher：The Crystallographic Society of Japan

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. Invited

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

2009.3

The Structure of Rat Liver Vault at 3.5 Angstrom Resolution Reviewed

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

SCIENCE 323 ( 5912 ) 384 - 388 2009.1

Language：English Publishing type：Research paper (scientific journal) Publisher：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 Reviewed

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

Science 49 ( Supplement 1 ) 2009.1

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

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

PEPTIDES 29 ( 12 ) 2110 - 2117 2008.12

Language：English Publishing type：Research paper (scientific journal) Publisher：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 Invited

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

2008.12

A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry Reviewed

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

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 64 525 - 531 2008.5

Language：English Publishing type：Research paper (scientific journal) Publisher：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 X-ray structure of the vault purified from rat liver(Invited Talk for Early Research in Biophysics Award,Early Research in Biophysics Award)(The 46th Annual Meeting of the Biophysical Society of Japan)

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

Seibutsu Butsuri 48 S21 2008

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

Seibutsu Butsuri 46 ( 2 ) S306 2006

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