研究者詳細 - 安永　卓生

論文 - 安永　卓生

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A visualization tool of biological macromolecular structures toward in slico microscopy

安永卓生

Annual Report of NIFS 2002 2003年03月

Archaeal Group II Chaperonin Mediates Protein Folding in the cis-Cavity Without a Detachable GroES-like Co-chaperonin 査読有り

Yoshida T.,Kawaguchi R.,Taguchi H.,Yoshida M.,Yasunaga T.,Wakabayashi T.,Yohda M.,Maruyama T

J. Mol. Biol. 315 ( 1 ) 73 - 85 2002年01月

Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin 査読有り国際誌

Yoshida T., Kawaguchi R., Taguchi H., Yoshida M., Yasunaga T., Wakabayashi T., Yohda M., Maruyama T.

Journal of Molecular Biology 315 ( 1 ) 73 - 85 2002年01月

記述言語：英語掲載種別：研究論文（学術雑誌）

Group II chaperonins of archaea and eukaryotes are distinct from group I chaperonins of bacteria. Whereas group I chaperonins require the co-chaperonin Cpn-10 or GroES for protein folding, no co-chaperonin has been known for group II. The protein folding mechanism of group II chaperonins is not yet clear. To understand this mechanism, we examined protein refolding by the recombinant α or β-subunit chaperonin homo-oligomer (α16mer and β16mer) from a hyperthermoplilic archaeum, Thermococcus strain KS-1, using a model substrate, green fluorescent protein (GFP). The α16mer and β16mer captured the non-native GFP and promoted its refolding without any co-chaperonin in an ATP dependent manner. A non-hydrolyzable ATP analog, AMP-PNP, induced the GFP refolding mediated by β16mer but not by the α16mer. A mutant α-subunit chaperonin homo-oligomer (trap-α) could capture the non-native protein but lacked the ability to refold it. Although trap-α suppressed ATP-dependent refolding of GFP mediated by α16mer or β16mer, it did not affect the AMP-PNP-dependent refolding. This indicated that the GFP refolding mediated by β16mer with AMP-PNP was not accessible to the trap-α. Gel filtration chromatography and a protease protection experiment revealed that this refolded GFP, in the presence of AMP-PNP, was associated with β16mer. After the completion of GFP refolding mediated by β16mer with AMP-PNP, addition of ATP induced an additional refolding of GFP. Furthermore, the β16mer preincubated with AMP-PNP showed the ability to capture the non-native GFP. These suggest that AMP-PNP induced one of two chaperonin rings (cis-ring) to close and induced protein refolding in this ring, and that the other ring (trans-ring) could capture the unfolded GFP which was refolded by adding ATP. The present data indicate that, in the group II chaperonin of Thermococcus strain KS-1, the protein folding proceeds in its cis-ring in an ATP-dependent fashion without any co-chaperonin. © 2002 Academic Press.

DOI： 10.1006/jmbi.2001.5220

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0036290267&origin=inward

Ca2+-induced switching of troponin on actin filaments revealed by electron cryo-microscopy 査読有り

Narita A.,Yasunaga T.,Ishikawa T.,Mayanagi K.,Wakabayashi T.

J. Mol. Biol. 308 ( 2 ) 241 - 261 2001年05月

Relocation of Cys374 of actin induced by labeling with fluorescent dyes 査読有り

Yasunaga T,Wakabayashi T.

J. Biochem. 129 ( 2 ) 201 - 204 2001年04月

1H1600 冷電界放出型電子銃、エネルギーフィルタ、高分解能高感度CCDを備えた透過型電子顕微鏡のアクチン・ミオシン硬直複合体構造解析への応用

安永卓生, 若林健之

生物物理 ( 一般社団法人日本生物物理学会 ) 40 ( 0 ) S63 2000年01月

クライオ電子顕微鏡法と逆投影法による細いフィラメントの三次元再構成招待有り査読有り

成田哲博, 石川尚, 真柳浩太, 安永卓生, 若林健之

生物物理 ( 一般社団法人日本生物物理学会 ) 38 ( 2 ) S62 1998年09月

28a-WE-1 クライオ電子顕微鏡法により可視化されたミオシン一分子の構造

安永卓生, 橋場修平, 若林健之

日本物理学会講演概要集 ( 一般社団法人日本物理学会 ) 52.1.3 ( 0 ) 759 1997年01月

28a-WE-4 細いフィラメントのクライオ電子顕微鏡写真からの、らせん対称性を仮定しない3次元構造解析へ向けて

成田哲博, 真柳浩太, 安永卓生, 若林健之

日本物理学会講演概要集 ( 一般社団法人日本物理学会 ) 52.1.3 ( 0 ) 760 1997年01月

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