| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2017-10-03 |
| タイトル |
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|
タイトル |
Role of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy |
| 言語 |
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|
言語 |
eng |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| ID登録 |
|
|
ID登録 |
10.24517/00010540 |
|
ID登録タイプ |
JaLC |
| 著者 |
Yamashita, Hayato
Inoue, Keiichi
Shibata, Mikihiro
Uchihashi, Takayuki
Sasaki, Jun
Kandori, Hideki
Ando, Toshio
|
| 著者別表示 |
柴田, 幹大
内橋, 貴之
安藤, 敏夫
|
| 提供者所属 |
|
|
内容記述タイプ |
Other |
|
内容記述 |
金沢大学ナノ生命科学研究所 |
| 書誌情報 |
Journal of Structural Biology
巻 184,
号 1,
p. 2-11,
発行日 2013-10-01
|
| ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
1047-8477 |
| NCID |
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収録物識別子タイプ |
NCID |
|
収録物識別子 |
AA10761632 |
| DOI |
|
|
関連タイプ |
isVersionOf |
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識別子タイプ |
DOI |
|
|
関連識別子 |
10.1016/j.jsb.2013.02.011 |
| 出版者 |
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出版者 |
Elsevier |
| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
Bacteriorhodopsin (bR) trimers form a two-dimensional hexagonal lattice in the purple membrane of Halobacterium salinarum. However, the physiological significance of forming the lattice has long been elusive. Here, we study this issue by comparing properties of assembled and non-assembled bR trimers using directed mutagenesis, high-speed atomic force microscopy (HS-AFM), optical spectroscopy, and a proton pumping assay. First, we show that the bonds formed between W12 and F135 amino acid residues are responsible for trimer-trimer association that leads to lattice assembly; the lattice is completely disrupted in both W12I and F135I mutants. HS-AFM imaging reveals that both crystallized D96N and non-crystallized D96N/W12I mutants undergo a large conformational change (i.e., outward E-F loop displacement) upon light-activation. However, lattice disruption significantly reduces the rate of conformational change under continuous light illumination. Nevertheless, the quantum yield of M-state formation, measured by low-temperature UV-visible spectroscopy, and proton pumping efficiency are unaffected by lattice disruption. From these results, we conclude that trimer-trimer association plays essential roles in providing bound retinal with an appropriate environment to maintain its full photo-reactivity and in maintaining the natural photo-reaction pathway. © 2013 Elsevier Inc. All rights reserved. |
| 著者版フラグ |
|
|
出版タイプ |
AM |
|
出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
| 関連URI |
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|
識別子タイプ |
URI |
|
|
関連識別子 |
http://www.elsevier.com/locate/issn/10478477 |
SC-PR-ANDO-T-JSB-2.pdf (1.0 MB)
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