Engineered Functional Recovery of Microbial Rhodopsin without Retinal-Binding Lysine

Yumeka Yamauchi, Masae Konno, Daichi Yamada, Kei Yura, Keiichi Inoue, Oded Béjà, Hideki Kandori

研究成果: Article

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

Fingerprint

Microbial Rhodopsins
Retinaldehyde
lysine
Lysine
Schiff Bases
Color
recovery
color
Recovery
imines
proteins
Proton Pumps
Rhodopsin
protons
Chromophores
mutations
Escherichia
linkages
helices
Escherichia coli

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

Yamauchi, Yumeka ; Konno, Masae ; Yamada, Daichi ; Yura, Kei ; Inoue, Keiichi ; Béjà, Oded ; Kandori, Hideki. / Engineered Functional Recovery of Microbial Rhodopsin without Retinal-Binding Lysine. :: Photochemistry and Photobiology. 2019.
@article{93a74abc4df14ad29edaa004a4971669,
title = "Engineered Functional Recovery of Microbial Rhodopsin without Retinal-Binding Lysine",
abstract = "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.",
author = "Yumeka Yamauchi and Masae Konno and Daichi Yamada and Kei Yura and Keiichi Inoue and Oded B{\'e}j{\`a} and Hideki Kandori",
year = "2019",
month = "1",
day = "1",
doi = "10.1111/php.13114",
language = "English",
journal = "Photochemistry and Photobiology",
issn = "0031-8655",
publisher = "Wiley-Blackwell",

}

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 -