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Microbial rhodopsins have advanced optogenetics since the discovery of channelrhodopsins almost two decades ago. During this time an abundance of microbial rhodopsins has been discovered, engineered, and improved for studies in neuroscience and other animal research fields. Optogenetic applications in plant research, however, lagged largely behind. Starting with light-regulated gene expression, optogenetics has slowly expanded into plant research. The recently established all-trans retinal production in plants now enables the use of many microbial opsins, bringing extra opportunities to plant research. In this review, we summarize the recent advances of rhodopsin-based plant optogenetics and provide a perspective for future use, combined with fluorescent sensors to monitor physiological parameters.
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http://dx.doi.org/10.1093/plphys/kiab338 | DOI Listing |
Structure
September 2025
HIT Center for Life Sciences, School of Life Science and Technology, Faculty of Life Sciences and Medicine, Harbin Institute of Technology, Harbin 150001, China; Frontiers Science Center for Matter Behave in Space Environment, Harbin Institute of Technology, Harbin 150001, China. Electronic address:
Rhodopsins typically harness light energy through the covalently bound retinal cofactor. However, some rhodopsins have lost this ability during evolution. In this issue of Structure, Kovalev et al.
View Article and Find Full Text PDFNat Microbiol
September 2025
Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan.
Microbial rhodopsins are photoreceptor proteins widely distributed in marine microorganisms that harness light energy and support marine ecosystems. While retinal is typically the sole chromophore in microbial rhodopsins, some proteorhodopsins, which are proton-pumping rhodopsins abundant in the ocean, use carotenoid antennae to transfer light energy to retinal. However, the mechanism by which carotenoids enhance rhodopsin functions remains unclear.
View Article and Find Full Text PDFbioRxiv
August 2025
Department of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706.
Opsins are highly abundant retinal proteins in the membranes of photoheterotrophic bacteria. However, some microbial genomes encode an but lack the gene for the final enzyme in retinal synthesis. To account for this paradox, we hypothesized that bacterial opsins play a role in membrane structure and/or biogenesis independent from their potential for light-driven signaling or proton pumping.
View Article and Find Full Text PDFChem Commun (Camb)
August 2025
Fritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 9190401, Israel.
Chrimson is a naturally occurring channelrhodopsin with one of the most red-shifted absorption maxima ( = 590 nm). This unique absorption makes it an ideal candidate for noninvasive optogenetic applications. The origin of the absorption maximum is thought to stem from a single deprotonated counterion near the Schiff base.
View Article and Find Full Text PDFBiochemistry (Mosc)
July 2025
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russia.
Recombinant proteorhodopsin ESR of the gram-positive bacterium isolated from permafrost deposits in northeastern Siberia binds retinal and acts as a light-dependent proton pump, but not much is known about its expression under natural conditions. In this work, expression of the gene in cultures grown under various conditions was studied by quantitative PCR. It has been discovered that cultivation on poor media at low temperatures contributes to a significant increase in the content of the corresponding mRNA.
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