研究者詳細 - 安永　卓生

論文 - 安永　卓生

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1P-114 アクチン-ミオシン硬直複合体の高分解能3次元像の獲得(筋肉(筋蛋白質・収縮),第47回日本生物物理学会年会)

Tsukada Yoshihiro, Wakabayashi Takeyuki, Yasunaga Takuo

生物物理 ( 一般社団法人日本生物物理学会 ) 49 ( supplement ) S81 2009年01月

1P-133 軸糸外腕ダイニンの構造及び微小管と複合体を形成する際のメカニズム(分子モーター,第47回日本生物物理学会年会)

Jin Mingyue, Takazaki Hiroko, Yasunaga Takuo

生物物理 ( 一般社団法人日本生物物理学会 ) 49 ( supplement ) S84 2009年01月

1P-136 カタユウレイボヤ軸糸外腕ダイニンの構造解析(分子モーター,第47回日本生物物理学会年会)

Harano Jun, Ueno Hironori, Mizuno Katsutoshi, Yasunaga Takuo, Inaba Kazuo, Hirose Keiko

生物物理 ( 一般社団法人日本生物物理学会 ) 49 ( supplement ) S84 2009年01月

Dynein pulls microtubules without rotating its stalk 査読有り国際誌

Ueno H., Yasunaga T., Shingyoji C., Hirose K.

Proceedings of the National Academy of Sciences of the United States of America ( Proceedings of the National Academy of Sciences ) 105 ( 50 ) 19702 - 19707 2008年12月

記述言語：英語掲載種別：研究論文（学術雑誌）

Dynein is a microtubule motor that powers motility of cilia and flagella. There is evidence that the relative sliding of the doublet microtubules is due to a conformational change in the motor domain that moves a microtubule bound to the end of an extension known as the stalk. A predominant model for the movement involves a rotation of the head domain, with its stalk, toward the microtubule plus end. However, stalks bound to microtubules have been difficult to observe. Here, we present the clearest views so far of stalks in action, by observing sea urchin, outer arm dynein molecules bound to microtubules, with a new method, "cryopositive stain" electron microscopy. The dynein molecules in the complex were shown to be active in in vitro motility assays. Analysis of the electron micrographs shows that the stalk angles relative to microtubules do not change significantly between the ADP·vanadate and no-nucleotide states, but the heads, together with their stalks, shift with respect to their A-tubule attachments. Our results disagree with models in which the stalk acts as a lever arm to amplify structural changes. The observed movement of the head and stalk relative to the tail indicates a new plausible mechanism, in which dynein uses its stalk as a grappling hook, catching a tubulin subunit 8 nm ahead and pulling on it by retracting a part of the tail (linker). © 2008 by The National Academy of Sciences of the USA.

DOI： 10.1073/pnas.0808194105

Scopus

CiNii Research

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=58149376460&origin=inward

Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T 査読有り国際誌

Kenji Murakami, Murray Stewart, Kayo Nozawa, Kumiko Tomii, Norio Kudou, Noriyuki Igarashi, Yasuo Shirakihara, Soichi Wakatsuki, Takuo Yasunaga, Takeyuki Wakabayashi

Proceedings of the National Academy of Sciences ( Proceedings of the National Academy of Sciences ) 105 ( 20 ) 7200 - 7205 2008年05月

記述言語：英語掲載種別：研究論文（学術雑誌）

<jats:p>Head-to-tail polymerization of tropomyosin is crucial for its actin binding, function in actin filament assembly, and the regulation of actin-myosin contraction. Here, we describe the 2.1 Å resolution structure of crystals containing overlapping tropomyosin N and C termini (TM-N and TM-C) and the 2.9 Å resolution structure of crystals containing TM-N and TM-C together with a fragment of troponin-T (TnT). At each junction, the N-terminal helices of TM-N were splayed, with only one of them packing against TM-C. In the C-terminal region of TM-C, a crucial water in the coiled-coil core broke the local 2-fold symmetry and helps generate a kink on one helix. In the presence of a TnT fragment, the asymmetry in TM-C facilitates formation of a 4-helix bundle containing two TM-C chains and one chain each of TM-N and TnT. Mutating the residues that generate the asymmetry in TM-C caused a marked decrease in the affinity of troponin for actin-tropomyosin filaments. The highly conserved region of TnT, in which most cardiomyopathy mutations reside, is crucial for interacting with tropomyosin. The structure of the ternary complex also explains why the skeletal- and cardiac-muscle specific C-terminal region is required to bind TnT and why tropomyosin homodimers bind only a single TnT. On actin filaments, the head-to-tail junction can function as a molecular swivel to accommodate irregularities in the coiled-coil path between successive tropomyosins enabling each to interact equivalently with the actin helix.</jats:p>

DOI： 10.1073/pnas.0801950105

CiNii Research

その他リンク： https://pnas.org/doi/pdf/10.1073/pnas.0801950105

Partially functional outer arm dynein in a novel Chlamydomonas mutant expressing a truncated γ heavy chain 査読有り

Liu Z.,Takazaki H.,Nakazawa Y.,Sakato M.,Yagi T.,Yasunaga T.,King S.M.,Kamiya R.

Eukaryotic Cell 7 1136 - 1145 2008年04月

Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T 査読有り

Murakami K.,Stewart M.,Nozawa K.,Tomii K.,Kudou N.,Igarashi N.,Shirakihara Y.,Wakatsuki S.,Yasunaga T.,Wakabayashi T.

ProNAS 105 ( 20 ) 7200 - 7205 2008年04月

Evaluation of a 2k CCD camera with an epitaxially-grown CsI scintillator for recording energy-filtered electron cryo-micrographs., Journal of Electron Microscopy, 57(3), 101-112 (2008) 査読有り

Yasunaga,T.,Wakabayashi,T.

Journal of Electron Microscopy 57 ( 3 ) 101 - 112 2008年04月

Dynein pulls microtubules without rotating its stalk 査読有り

Ueno H.,Yasunaga T.,Shigyoji,C.,Hirose K

ProNAS 105 19702 - 19707 2008年04月

Expression of excess receptors and negative feedback control of signal pathways are required for rapid activation and prompt cessation of signal transduction 査読有り

Kobayashi,H.,Azuma,R.,Yasunaga T.

Cell Communication and Signaling 7 ( 3 ) 2008年03月

ナノイメージングを可能にする顕微鏡法・電子顕微鏡を用いたナノイメージング招待有り

安永卓生

ナノイメージング((株)NTS) 2008年01月

1P-143 ダイニン・微小管複合体の構造学的研究(分子モーター(1),第46回日本生物物理学会年会)

Ueno Hironori, Yasunaga Takuo, Shingyoji Chikako, Hirose Keiko

生物物理 ( 一般社団法人日本生物物理学会 ) 48 ( supplement ) S43 2008年01月

第一編ナノイメージングを可能にする顕微鏡法・第3章電子顕微鏡を用いたナノイメージング招待有り

安永卓生

ナノイメージング((株)NTS) 15 2008年01月

A genetically　encoded metallothionein tag enabling efficient protein detection by electron microscopy 査読有り

Nishino Y,Yasunaga T,Miyazawa A

Journal of Electron Microscopy 56 ( 3 ) 93 - 101 2007年08月

A genetically encoded metallothionein tag enabling efficient protein detection by electron microscopy 査読有り

Nishino Y., Yasunaga T., Miyazawa A.

Journal of Electron Microscopy 56 ( 3 ) 93 - 101 2007年06月

記述言語：英語掲載種別：研究論文（学術雑誌）

The observation of biological materials by transmission electron microscopy (TEM) frequently requires the use of negative staining and/or immuno-gold labeling to visualize or identify the specimen, but these techniques are limited. In contrast, genetic labeling with green fluorescent protein (GFP) and its homologs have led to rapid advances in the observation of proteins of interest in cells by light microscopy (LM). These fluorescent tags allow for the visualization of dynamic processes in live cells without the use of secondary reagents. Here, we report the development of an artificial metalloprotein fusion protein expressed in Escherichia coli grown in Cd2+-containing medium that allows for efficient protein detection by TEM without additional staining steps. We linked the subunits of the bacterial 14-mer protein GroEL with three repeats of metallothionein (3MT). The 3MT-fused GroEL (GroEL-14(3MT)) was successfully expressed in E. coli, and the purified protein included 250 cadmium atoms per molecule on average. Cd2+-bound GroEL-14(3MT) was detected by TEM in the absence of negative staining on a carbon grid, and the particle densities of GroEL-14(3MT) were much greater than those of untagged GroEL in vitreous ice. Taken together, our data indicate that the 3MT tag provides a promising means of allowing the identification of oligomeric proteins isolated from cells in the absence of other detection techniques. © The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Microscopy. All rights reserved.

DOI： 10.1093/jmicro/dfm008

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=35948943072&origin=inward

Domains 16 and 17 of tropoelastin in elastic fiber formation 査読有り

Wachi H.,Sato F.,Nakazawa J.,Nonaka R.,Szabo Z.,Urban Z.,Yasunaga T.,Maeda I.,Okamoto K.,Starcher B.C.,Li D.Y.,Mecham R.P.,Seyama Y.

Biochemical Journal. 402 60 - 70 2007年04月

An actin homolog of the archaeon Thermoplasma acidophilum that retains the ancient trait of eukaryotic actin 査読有り

Hara F.,Yamashiro K.,Nemoto N.,Ohta Y,Yokobori S,Yasunaga T.,Hisanaga S. and Yamagishi A

J. Bacteriology. 189 ( 5 ) 2039 - 2045 2007年04月

電子顕微鏡画像解析ソフトウェア統合環境Eosの試み招待有り査読有り

安永　卓生

顕微鏡 42 ( 3 ) 2007年04月

1P054 単粒子解析のための粒子投影方向決定の新手法 : シノグラムライン特徴量とその応用(蛋白質(計測解析の方法論),ポスター発表,第45回日本生物物理学会年会)

村山涼子, 安永卓生

生物物理 ( 一般社団法人日本生物物理学会 ) 47 ( supplement ) S37 2007年01月

電子顕微鏡画像解析ソフトウェア統合環境査読有り

安永卓生

Eosの試み 42 214 - 216 2007年01月

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