Identification of Cyanobacteriochromes Detecting Far-Red Light
Abstract
The opacity of mammalian tissue to visible light and the strong attenuation of infrared light by water at ≥900 nm have contributed to growing interest in the development of far-red and near-infrared absorbing tools for visualizing and actuating responses within live cells. Here we report the discovery of cyanobacteriochromes (CBCRs) responsive to light in this far-red window. CBCRs are linear tetrapyrrole (bilin)-based light sensors distantly related to plant phytochrome sensors. Our studies reveal far-red (λmax = 725–755 nm)/orange (λmax = 590–600 nm) and far-red/red (λmax = 615–685 nm) photoswitches that are small (<200 amino acids) and can be genetically reconstituted in living cells. Phylogenetic analysis and characterization of additional CBCRs demonstrated that far-red/orange CBCRs evolved after a complex transition from green/red CBCRs known for regulating complementary chromatic acclimation. Incorporation of different bilin chromophores demonstrated that tuning mechanisms responsible for red-shifted chromophore absorption act at the A-, B-, and/ or C-rings, whereas photoisomerization occurs at the D-ring. Two such proteins exhibited detectable fluorescence extending well into the near-infrared region. In conclusion, this work extends the spectral window of CBCRs to the edge of the infrared, raising the possibility of using CBCRs in synthetic biology applications in the far-red region of themore »
- Authors:
-
- Department of Molecular and Cellular Biology, University of California, Davis, California 95616, United States
- Publication Date:
- Research Org.:
- Univ. of California, Davis, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1260055
- Alternate Identifier(s):
- OSTI ID: 1267164
- Grant/Contract Number:
- SC0002395
- Resource Type:
- Journal Article: Published Article
- Journal Name:
- Biochemistry
- Additional Journal Information:
- Journal Name: Biochemistry Journal Volume: 55 Journal Issue: 28; Journal ID: ISSN 0006-2960
- Publisher:
- American Chemical Society
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Rockwell, Nathan C., Martin, Shelley S., and Lagarias, J. Clark. Identification of Cyanobacteriochromes Detecting Far-Red Light. United States: N. p., 2016.
Web. doi:10.1021/acs.biochem.6b00299.
Rockwell, Nathan C., Martin, Shelley S., & Lagarias, J. Clark. Identification of Cyanobacteriochromes Detecting Far-Red Light. United States. https://doi.org/10.1021/acs.biochem.6b00299
Rockwell, Nathan C., Martin, Shelley S., and Lagarias, J. Clark. 2016.
"Identification of Cyanobacteriochromes Detecting Far-Red Light". United States. https://doi.org/10.1021/acs.biochem.6b00299.
@article{osti_1260055,
title = {Identification of Cyanobacteriochromes Detecting Far-Red Light},
author = {Rockwell, Nathan C. and Martin, Shelley S. and Lagarias, J. Clark},
abstractNote = {The opacity of mammalian tissue to visible light and the strong attenuation of infrared light by water at ≥900 nm have contributed to growing interest in the development of far-red and near-infrared absorbing tools for visualizing and actuating responses within live cells. Here we report the discovery of cyanobacteriochromes (CBCRs) responsive to light in this far-red window. CBCRs are linear tetrapyrrole (bilin)-based light sensors distantly related to plant phytochrome sensors. Our studies reveal far-red (λmax = 725–755 nm)/orange (λmax = 590–600 nm) and far-red/red (λmax = 615–685 nm) photoswitches that are small (<200 amino acids) and can be genetically reconstituted in living cells. Phylogenetic analysis and characterization of additional CBCRs demonstrated that far-red/orange CBCRs evolved after a complex transition from green/red CBCRs known for regulating complementary chromatic acclimation. Incorporation of different bilin chromophores demonstrated that tuning mechanisms responsible for red-shifted chromophore absorption act at the A-, B-, and/ or C-rings, whereas photoisomerization occurs at the D-ring. Two such proteins exhibited detectable fluorescence extending well into the near-infrared region. In conclusion, this work extends the spectral window of CBCRs to the edge of the infrared, raising the possibility of using CBCRs in synthetic biology applications in the far-red region of the spectrum.},
doi = {10.1021/acs.biochem.6b00299},
url = {https://www.osti.gov/biblio/1260055},
journal = {Biochemistry},
issn = {0006-2960},
number = 28,
volume = 55,
place = {United States},
year = {Sat Jul 02 00:00:00 EDT 2016},
month = {Sat Jul 02 00:00:00 EDT 2016}
}
Web of Science
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