東京工業大学 · 生化学・遺伝学・分子生物学
Hideki Taguchi教授の研究室は、酸化物ペロブスカイトの低温合成から、シャペロニンをはじめとするシャペロン・タンパク質の構造機能解明、酵母プリオンの凝集様式と動的挙動の高分解能イメージングまで、分子生物学的・材料科学的アプローチを融合した多様な研究を展開しています。特に、原子間力顕微鏡や電子顕微鏡を用いたプリオンのリアルタイム観察や、ATP依存的シャペロンの機能メカニズムの解明が特徴です。細胞内でのタンパク質凝集の動的挙動を単細胞レベルで可視化する技術的革新にも貢献しています。
Figures are computed from collected data and may differ slightly.
Perovskite‐type (La 1‐ x Sr x )MnO 3 (0 x 0.3) was synthesized through the sol–gel process at low temperature (400° to 500°C). Poly(acrylic acid) (PAA) was used to make a gel from an aqueous solution of lanthanum, strontium, and manganese nitrates. The particle‐diameter distribution of the manganites had a maximum value of 0.3 to 0.7 μ m, and a specific surface area of about 17.5 to 23.5 m 2 /g.
A chaperonin has been purified from a thermophilic bacterium, Thermus thermophilus. It consists of two kinds of proteins with approximate Mr 58,000 and 10,000 and shows a 7-fold rotational symmetry from the top view and a "football"-like shape from the side view under the electron microscopic view. Its weak ATPase activity is inhibited by sulfite and activated by bicarbonate. ATP causes change of its mobility in nondenaturating polyacrylamide gel electrophoresis. The T. thermophilus chaperonin c
Yeast prion [PSI+] is caused by aggregated structures of the Sup35 protein. Although Sup35 forms typical amyloid fibrils in vitro, there is no direct evidence for the fibrillar structures of Sup35 in vivo. We analyzed [PSI+] cells in which Sup35 fused with green fluorescent protein (GFP) formed aggregates visible by fluorescence microscopy using thin-section electron microscopy (EM). Rapid-freeze EM combined with an immunogold-labeling technique as well as correlative light EM, which allows high
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