抄録
Definition of rhodopsin is the retinal-binding membrane protein with the Schiff base linkage at a lysine on the 7th transmembrane helix. However, ~ 600 microbial rhodopsins lack retinal-binding lysine at the corresponding position (Rh-noK) among ~ 5500 known microbial rhodopsins, suggesting that Rh-noK has each functional role without chromophore. Here, we report successful functional recovery of Rh-noK. Two Rh-noKs from bacteria were heterologously expressed in Escherichia coli, which exhibited no color. When retinal-binding lysine was introduced, one of them gained visible color. Additional mutation of the Schiff base counterion further gained proton-pumping activity. Successful engineered functional recovery such as visible color and proton-pump activity suggests that the Rh-noK protein forms a characteristic structure of microbial rhodopsins.
| 元の言語 | English |
|---|---|
| ジャーナル | Photochemistry and Photobiology |
| DOI | |
| 出版物ステータス | Published - 2019 1 1 |
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ASJC Scopus subject areas
- Biochemistry
- Physical and Theoretical Chemistry
これを引用
Engineered Functional Recovery of Microbial Rhodopsin without Retinal-Binding Lysine. / Yamauchi, Yumeka; Konno, Masae; Yamada, Daichi; Yura, Kei; Inoue, Keiichi; Béjà, Oded; Kandori, Hideki.
：: Photochemistry and Photobiology, 01.01.2019.研究成果: Article
}
TY - JOUR
T1 - Engineered Functional Recovery of Microbial Rhodopsin without Retinal-Binding Lysine
AU - Yamauchi, Yumeka
AU - Konno, Masae
AU - Yamada, Daichi
AU - Yura, Kei
AU - Inoue, Keiichi
AU - Béjà, Oded
AU - Kandori, Hideki
PY - 2019/1/1
Y1 - 2019/1/1
N2 - Definition of rhodopsin is the retinal-binding membrane protein with the Schiff base linkage at a lysine on the 7th transmembrane helix. However, ~ 600 microbial rhodopsins lack retinal-binding lysine at the corresponding position (Rh-noK) among ~ 5500 known microbial rhodopsins, suggesting that Rh-noK has each functional role without chromophore. Here, we report successful functional recovery of Rh-noK. Two Rh-noKs from bacteria were heterologously expressed in Escherichia coli, which exhibited no color. When retinal-binding lysine was introduced, one of them gained visible color. Additional mutation of the Schiff base counterion further gained proton-pumping activity. Successful engineered functional recovery such as visible color and proton-pump activity suggests that the Rh-noK protein forms a characteristic structure of microbial rhodopsins.
AB - Definition of rhodopsin is the retinal-binding membrane protein with the Schiff base linkage at a lysine on the 7th transmembrane helix. However, ~ 600 microbial rhodopsins lack retinal-binding lysine at the corresponding position (Rh-noK) among ~ 5500 known microbial rhodopsins, suggesting that Rh-noK has each functional role without chromophore. Here, we report successful functional recovery of Rh-noK. Two Rh-noKs from bacteria were heterologously expressed in Escherichia coli, which exhibited no color. When retinal-binding lysine was introduced, one of them gained visible color. Additional mutation of the Schiff base counterion further gained proton-pumping activity. Successful engineered functional recovery such as visible color and proton-pump activity suggests that the Rh-noK protein forms a characteristic structure of microbial rhodopsins.
UR - http://www.scopus.com/inward/record.url?scp=85068527423&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85068527423&partnerID=8YFLogxK
U2 - 10.1111/php.13114
DO - 10.1111/php.13114
M3 - Article
AN - SCOPUS:85068527423
JO - Photochemistry and Photobiology
JF - Photochemistry and Photobiology
SN - 0031-8655
ER -