LOV to BLUF: Flavoprotein Contributions to the Optogenetic Toolkit

Christie, John M.; Gawthorne, Jayde A.; Young, Gillian; Fraser, Niall J.; Roe, Andrew J.

doi:10.1093/mp/sss020

Cited by 122 publications

(134 citation statements)

References 135 publications

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“…Importantly, the analysis readily distinguishes a LOV domain from its most closely related protein domains, which include non-LOV PAS domains (including PYP, "photoactive yellow protein") and other flavoproteins, including BLUF domain photoreceptors ("Blue-Light Using FAD") (18,26,(31)(32)(33) (Fig. 2C and Dataset S1).…”

Section: Resultsmentioning

confidence: 99%

Functional and topological diversity of LOV domain photoreceptors

Glantz

Carpenter

Melkonian

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

132

155

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Light-oxygen-voltage sensitive (LOV) flavoproteins are ubiquitous photoreceptors that mediate responses to environmental cues. Photosensory inputs are transduced into signaling outputs via structural rearrangements in sensor domains that consequently modulate the activity of an effector domain or multidomain clusters. Establishing the diversity in effector function and sensor-effector topology will inform what signaling mechanisms govern light-responsive behaviors across multiple kingdoms of life and how these signals are transduced. Here, we report the bioinformatics identification of over 6,700 candidate LOV domains (including over 4,000 previously unidentified sequences from plants and protists), and insights from their annotations for ontological function and structural arrangements. Motif analysis identified the sensors from ∼42 million ORFs, with strong statistical separation from other flavoproteins and non-LOV members of the structurally related Per-aryl hydrocarbon receptor nuclear translocator (ARNT)-Sim family. Conserved-domain analysis determined putative light-regulated function and multidomain topologies. We found that for certain effectors, sensor-effector linker length is discretized based on both phylogeny and the preservation of α-helical heptad repeats within an extended coiled-coil linker structure. This finding suggests that preserving sensor-effector orientation is a key determinant of linker length, in addition to ancestry, in LOV signaling structure-function. We found a surprisingly high prevalence of effectors with functions previously thought to be rare among LOV proteins, such as regulators of G protein signaling, and discovered several previously unidentified effectors, such as lipases. This work highlights the value of applying genomic and transcriptomic technologies to diverse organisms to capture the structural and functional variation in photosensory proteins that are vastly important in adaptation, photobiology, and optogenetics.photoreceptors | LOV | flavoproteins | optogenetics

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Section: Resultsmentioning

confidence: 99%

Functional and topological diversity of LOV domain photoreceptors

Glantz

Carpenter

Melkonian

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

132

155

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“…In this context, the LOV domain serves as a modular photoswitch, placing protein activities, such as kinases, phosphodiesterases and DNA-binding under light control. This modularity of regulation has lately been exploited to create artificial photoswitches for the optical control of biological processes in an emerging field known as optogenetics [8].…”

Section: Lov-domain Function and Fluorescencementioning

confidence: 99%

“…For example, DsFbFP, derived from a LOV-coding sequence isolated from the marine a-proteobacterium Dinoroseobacter shibae, exhibits improved fluorescence over PpFbFP [20 ], whilst Crei-LOV, obtained from a photoreceptor protein from the fresh water alga Chlamydomonas reinhardtii, shows enhancements in brightness, photostability and pH tolerance over LOV-based FPs such as iLOV [22]. Thermal stability enhancements in reporter activity have also been reported for CreiLOV, through targeted mutagenesis of EcFbFP [23] and from genome mining for LOV-coding sequences from thermotolerant organisms [8]. Disappointingly, LOV-coding sequences appear to be absent from extremophiles [24], thus limiting the opportunity to exploit this source of genetic diversity.…”

Section: Natural Diversitymentioning

confidence: 99%

LOV-based reporters for fluorescence imaging

Buckley

Petersen

Roe

et al. 2015

Current Opinion in Chemical Biology

106

102

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Chromophore-binding domains from plant and bacterial photoreceptor proteins have recently gathered increasing attention as new sources of genetically encoded fluorescent proteins (FPs). In particular, FPs based on the flavin-binding LOV (light, oxygen, or voltage sensing) domain offer advantages over green fluorescent protein (GFP) owing to their smaller size, pH and thermal stability, utility under anaerobic conditions and their ability to generate reactive oxygen species. This review focuses on the potential applications of this emerging class of fluorescent reporters, discusses the advantages and limitations of LOV-based FPs, whilst offering insights regarding the further development of this technology for bioimaging and photodynamic therapy.

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“…Отметим, что помимо использования фото-тропинового LOV2 в качестве светозависимого ре-гулятора биологических процессов, на основе этого домена созданы флуоресцентные репортерные мо-лекулы [2,27,30]. Они успешно применяются для контроля популяций бактерий в анаэробных усло-виях либо вирусных инфекций растений.…”

Section: применение Lov-и Bluf-фотосенсоров в оптогенетических системахunclassified