Conversion of microbial rhodopsins

insights into functionally essential elements and rational protein engineering

Akimasa Kaneko, Keiichi Inoue, Keiichi Kojima, Hideki Kandori, Yuki Sudo

Research output: Contribution to journalReview article

7 Citations (Scopus)

Abstract

Technological progress has enabled the successful application of functional conversion to a variety of biological molecules, such as nucleotides and proteins. Such studies have revealed the functionally essential elements of these engineered molecules, which are difficult to characterize at the level of an individual molecule. The functional conversion of biological molecules has also provided a strategy for their rational and atomistic design. The engineered molecules can be used in studies to improve our understanding of their biological functions and to develop protein-based tools. In this review, we introduce the functional conversion of membrane-embedded photoreceptive retinylidene proteins (also called rhodopsins) and discuss these proteins mainly on the basis of results obtained from our own studies. This information provides insights into the molecular mechanism of light-induced protein functions and their use in optogenetics, a technology which involves the use of light to control biological activities.

Original languageEnglish
Pages (from-to)861-876
Number of pages16
JournalBiophysical Reviews
Volume9
Issue number6
DOIs
Publication statusPublished - Dec 1 2017

Fingerprint

Microbial Rhodopsins
Protein Engineering
Proteins
Optogenetics
Light
Rhodopsin
Nucleotides
Technology
Membranes

Keywords

  • Energy conversion
  • Membrane protein
  • Retinal
  • Rhodopsin
  • Signal transduction

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology

Cite this

Conversion of microbial rhodopsins : insights into functionally essential elements and rational protein engineering. / Kaneko, Akimasa; Inoue, Keiichi; Kojima, Keiichi; Kandori, Hideki; Sudo, Yuki.

In: Biophysical Reviews, Vol. 9, No. 6, 01.12.2017, p. 861-876.

Research output: Contribution to journalReview article

@article{e72f2596d62d42dd8fa52eeaf4484009,
title = "Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering",
abstract = "Technological progress has enabled the successful application of functional conversion to a variety of biological molecules, such as nucleotides and proteins. Such studies have revealed the functionally essential elements of these engineered molecules, which are difficult to characterize at the level of an individual molecule. The functional conversion of biological molecules has also provided a strategy for their rational and atomistic design. The engineered molecules can be used in studies to improve our understanding of their biological functions and to develop protein-based tools. In this review, we introduce the functional conversion of membrane-embedded photoreceptive retinylidene proteins (also called rhodopsins) and discuss these proteins mainly on the basis of results obtained from our own studies. This information provides insights into the molecular mechanism of light-induced protein functions and their use in optogenetics, a technology which involves the use of light to control biological activities.",
keywords = "Energy conversion, Membrane protein, Retinal, Rhodopsin, Signal transduction",
author = "Akimasa Kaneko and Keiichi Inoue and Keiichi Kojima and Hideki Kandori and Yuki Sudo",
year = "2017",
month = "12",
day = "1",
doi = "10.1007/s12551-017-0335-x",
language = "English",
volume = "9",
pages = "861--876",
journal = "Biophysical Reviews",
issn = "1867-2450",
publisher = "Springer Verlag",
number = "6",

}

TY - JOUR

T1 - Conversion of microbial rhodopsins

T2 - insights into functionally essential elements and rational protein engineering

AU - Kaneko, Akimasa

AU - Inoue, Keiichi

AU - Kojima, Keiichi

AU - Kandori, Hideki

AU - Sudo, Yuki

PY - 2017/12/1

Y1 - 2017/12/1

N2 - Technological progress has enabled the successful application of functional conversion to a variety of biological molecules, such as nucleotides and proteins. Such studies have revealed the functionally essential elements of these engineered molecules, which are difficult to characterize at the level of an individual molecule. The functional conversion of biological molecules has also provided a strategy for their rational and atomistic design. The engineered molecules can be used in studies to improve our understanding of their biological functions and to develop protein-based tools. In this review, we introduce the functional conversion of membrane-embedded photoreceptive retinylidene proteins (also called rhodopsins) and discuss these proteins mainly on the basis of results obtained from our own studies. This information provides insights into the molecular mechanism of light-induced protein functions and their use in optogenetics, a technology which involves the use of light to control biological activities.

AB - Technological progress has enabled the successful application of functional conversion to a variety of biological molecules, such as nucleotides and proteins. Such studies have revealed the functionally essential elements of these engineered molecules, which are difficult to characterize at the level of an individual molecule. The functional conversion of biological molecules has also provided a strategy for their rational and atomistic design. The engineered molecules can be used in studies to improve our understanding of their biological functions and to develop protein-based tools. In this review, we introduce the functional conversion of membrane-embedded photoreceptive retinylidene proteins (also called rhodopsins) and discuss these proteins mainly on the basis of results obtained from our own studies. This information provides insights into the molecular mechanism of light-induced protein functions and their use in optogenetics, a technology which involves the use of light to control biological activities.

KW - Energy conversion

KW - Membrane protein

KW - Retinal

KW - Rhodopsin

KW - Signal transduction

UR - http://www.scopus.com/inward/record.url?scp=85037133773&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85037133773&partnerID=8YFLogxK

U2 - 10.1007/s12551-017-0335-x

DO - 10.1007/s12551-017-0335-x

M3 - Review article

VL - 9

SP - 861

EP - 876

JO - Biophysical Reviews

JF - Biophysical Reviews

SN - 1867-2450

IS - 6

ER -