Plants with genetically encoded autoluminescence

Mitiouchkina, Tatiana; Mishin, Alexander S.; Somermeyer, Louisa Gonzalez; Markina, Nadezhda M.; Chepurnyh, Tatiana V.; Guglya, Elena B.; Karataeva, T; Palkina, Kseniia A.; Shakhova, Ekaterina S.; Fakhranurova, Liliia I.; Chekova, Sofia V.; Tsarkova, Aleksandra S.; Golubev, Yaroslav V.; Negrebetsky, Vadim V.; Dolgushin, S. A.; Shalaev, Pavel V.; Shlykov, Dmitry; Melnik, Olesya A.; Shipunova, Victoria O.; Deyev, Sergey M.; Bubyrev, Andrey I.; Pushin, Alexander; Choob, Vladimir V.; Dolgov, Sergey; Kondrashov, Fyodor A.; Yampolsky, Ilia V.; Sarkisyan, Karen S.

doi:10.1038/s41587-020-0500-9

Cited by 102 publications

(119 citation statements)

References 16 publications

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“…Plant cells are often light-sensitive, and observation with fluorescent labels can affect their activity owing to the intense illumination by the excitation light. Recently, the development of autoluminescent plants [ 28 ] has made it possible to observe plants without the need for the excitation of light or the addition of substrates. The smartphone microscope, which can easily observe the bioluminescence, makes it suitable for plant imaging.…”

Section: Discussionmentioning

confidence: 99%

Smartphone-Based Portable Bioluminescence Imaging System Enabling Observation at Various Scales from Whole Mouse Body to Organelle

Hattori

Shirane²,

Matsuda

et al. 2020

Sensors

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Current smartphones equipped with high-sensitivity and high-resolution sensors in the camera can respond to the needs of low-light imaging, streaming acquisition, targets of various scales, etc. Therefore, a smartphone has great potential as an imaging device even in the scientific field and has already been introduced into biomolecular imaging using fluorescence tags. However, owing to the necessity of an excitation light source, fluorescence methods impair its mobility. Bioluminescence does not require illumination; therefore, imaging with a smartphone camera is compact and requires minimal devices, thus making it suitable for personal and portable imaging devices. Here, we report smartphone-based methods to observe biological targets in various scales using bioluminescence. In particular, we demonstrate, for the first time, that bioluminescence can be observed in an organelle in a single living cell using a smartphone camera by attaching a detachable objective lens. Through capturing color changes with the camera, changes in the amount of target molecules was detected using bioluminescent indicators. The combination of bioluminescence and a mobile phone makes possible a compact imaging system without an external light source and expands the potential of portable devices.

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Section: Discussionmentioning

confidence: 99%

Smartphone-Based Portable Bioluminescence Imaging System Enabling Observation at Various Scales from Whole Mouse Body to Organelle

Hattori

Shirane²,

Matsuda

et al. 2020

Sensors

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“…We propose that they all may participate in the bioluminescence‐related metabolism. It includes: (i) metabolic precursors of the Henlea luciferin, like hispidin and caffeic acid are the precursors of 3‐hydroxyhispidin (luciferin) in fungi, [42,43] (ii) side‐products with unknown function, see a number of compounds from Fridericia heliota , [44] (iii) oxyluciferin, the product of enzymatic oxidation of luciferin accompanied by light emission, [3,36,45] and (iv) the product of non‐enzymatic degradation of luciferin [36,46] . Henlea sp .…”

Section: Discussionmentioning

confidence: 99%

α‐C‐Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp.

et al. 2020

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Cold extract from bioluminescent earthworm Henlea sp. was studied by HPLC, 1D and 2D NMR and LC-HRMS analysis. An abundant structural analog of the luciferin was isolated and identified as α-C-mannosyltryptophan (ManTrp), the product of unusual C2-glycosylation found earlier in humans, ascidians and other animals. Two compounds in cold extract (P300b, P300c) were characterized as C2-substituted derivatives of tryptophan. We hypothesize that a series of tryptophancontaining compounds are possible participants of bioluminescence-related metabolism in Henlea sp.

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“…The ability to use NADH is an attractive feature for the usage of the enzyme as a biocatalyst as NADPH is relatively costly. Furthermore, enzyme variants optimized for the use of both cofactors may boost the performance of fungal luminescent systems in recombinant organisms, such as engineered luminescent plants (17).…”

Section: Discussionmentioning

confidence: 99%

“…Recently, a plant was equipped with the fungal genes responsible for luminescence. Upon insertion of the four mentioned genes from the bioluminescent mushroom Neonothopanus nambi into the DNA of tobacco plants, luminous plants were created (17). The functioning of the fungal system in tobacco plants confirms that it can simply be fueled with the plant endogenous substrate caffeic acid.…”

Section: Introductionmentioning

confidence: 93%

Substrate binding tunes the reactivity of hispidin 3-hydroxylase, a flavoprotein monooxygenase involved in fungal bioluminescence

Tong

Trajković

Savino

et al. 2020

Journal of Biological Chemistry

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Fungal bioluminescence was recently shown to depend on a unique oxygen-dependent system of several enzymes. However, the identities of the enzymes did not reveal the full biochemical details of this process, as the enzymes do not bear resemblance to those of other luminescence systems, and thus the properties of the enzymes involved in this fascinating process are still unknown. Here, we describe the characterization of the penultimate enzyme in the pathway, hispidin 3-hydroxylase, from the luminescent fungus Mycena chlorophos (McH3H), which catalyzes the conversion of hispidin to 3-hydroxyhispidin. 3‑Hydroxyhispidin acts as a luciferin substrate in luminescent fungi. McH3H was heterologously expressed in Escherichia coli and purified by affinity chromatography with a yield of 100 mg/l. McH3H was found to be a single component monomeric NAD(P)H-dependent FAD-containing monooxygenase having a preference for NADPH. Through site-directed mutagenesis, based on a modeled structure, mutant enzymes were created that are more efficient with NADH. Except for identifying the residues that tune cofactor specificity, these engineered variants may also help in developing new hispidin-based bioluminescence applications. We confirmed that addition of hispidin to McH3H led to the formation of 3-hydroxy-hispidin as sole aromatic product. Rapid kinetic analysis revealed that reduction of the flavin cofactor by NADPH is boosted by hispidin binding by nearly 100-fold. Similar to other class A flavoprotein hydroxylases, McH3H did not form a stable hydro-peroxyflavin intermediate. These data suggest a mechanism by which the hydroxylase is tuned for converting hispidin into the fungal luciferin.

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Plants with genetically encoded autoluminescence

Cited by 102 publications

References 16 publications

Smartphone-Based Portable Bioluminescence Imaging System Enabling Observation at Various Scales from Whole Mouse Body to Organelle

Smartphone-Based Portable Bioluminescence Imaging System Enabling Observation at Various Scales from Whole Mouse Body to Organelle

α‐C‐Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp.

Substrate binding tunes the reactivity of hispidin 3-hydroxylase, a flavoprotein monooxygenase involved in fungal bioluminescence

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