Toolkit Items

CRY1 is a blue-light-sensing cryptochrome protein from the Arabidopsis cryptochrome family, and the name cry1 is also used for a Drosophila-like insect cryptochrome gene family. The supplied evidence indicates that CRY1 mediates blue light responses, contributes to regulation of early blue light-induced genes, and has functional overlap with CRY2.

The LOV2 domain from Avena sativa phototropin-1 is a photosensitive protein domain used as a light-responsive module in optogenetic engineering. It has been fused to other functional elements, including a Keratin 8 2B2-derived peptide in PA-dIF, to confer photoactivatable regulation.

The Arabidopsis thaliana phototropin 1 LOV2 domain is a blue-light-sensing protein domain from phototropin 1 whose dark-adapted crystal structure has been determined. In this state, the domain is dimeric and contains an N-terminal A'α helix and a C-terminal Jα helix that contribute to coiled-coil-mediated dimerization.

Phot2 is the Arabidopsis thaliana phototropin 2 blue-light receptor represented here as a protein-domain-level light-responsive tool candidate. The supplied evidence links phot2 to blue-light-dependent transcriptional regulation as a subsidiary contributor and to photomorphogenic cotyledon expansion.

Cyanobacteriochromes are cyanobacterial photoreceptor proteins built around a bilin-binding GAF domain related to phytochromes. They sense colors of light distinct from canonical phytochromes and have been applied in synthetic biology, including as the basis for an engineered near-infrared fluorescent protein tag.

Encephalopsin is an opsin-family protein domain reported in a 2013 PLoS Biology study to render neuronal cells light-sensitive. The provided evidence supports a light-responsive role but does not specify its molecular photochemistry, signaling partners, or spectral properties.

LOV1 is a blue-light-sensing Light-Oxygen-Voltage photosensor domain from Chlamydomonas reinhardtii that occurs in phototropin receptors. In phototropins, LOV1 is paired with LOV2 and a C-terminal serine/threonine kinase domain within a multidomain light-regulated signaling protein.

LOV domain–based photoswitches are protein-domain tools built from LOV photosensory modules that respond to light. The cited 2010 Nature Methods study reports rational improvement of these light-responsive photoswitches.

The phototropin 1 LOV1 domain is a blue-light-sensing LOV domain from Arabidopsis phototropin 1 that was tested in domain complementation assays for phototropism and leaf expansion. In the cited Arabidopsis study, the phot1 LOV1 domain did not complement either phenotype.

The phototropin 2 LOV1 domain (phot2 LOV1) is a light-sensing protein domain from Arabidopsis phototropin 2. In Arabidopsis, this domain was reported to complement phototropism to a considerable level, indicating functional activity in a domain-based complementation context.

The phototropin 2 LOV2 domain is a Light, Oxygen, or Voltage photosensory domain from Arabidopsis phototropin 2. In Arabidopsis, this domain has a major role in phototropism and leaf expansion.

TMT-opsins are vertebrate nonvisual photopigments identified in brain interneurons and motorneurons, including cells co-expressing VAL-opsins. Reported expression patterns and isolated adult tectal slice physiology associate TMT-opsin-expressing neuronal populations with intrinsic light responsiveness in the fish brain.

VAL-opsins are vertebrate nonvisual photopigments identified in brain tissue and studied in the context of photosensory interneurons and motorneurons. The cited evidence links VAL-opsin-positive neuronal populations to light-responsive tectal interneurons and to co-expression with TMT-opsins in distinct interneurons and motorneurons.

The bacteriophytochrome sensor unit is a light-sensing protein domain discussed in photoreceptor histidine kinases. A 2019 review places it among receptor sensor units that use recurring signaling strategies for light-driven signal transduction.

The bilin-binding GAF domain is the photosensory domain shared by cyanobacteriochromes and phytochromes. In cyanobacteriochromes, this domain binds a bilin chromophore and supports light sensing across colors extending beyond the red/far-red range.

Light-based real-time feedback control is an engineering method for microbial cell culture that uses engineered bacterial light sensors together with synthetic circuit-tuning practices. The cited literature describes it as an application framework built on optogenetic sensing and control rather than as a single molecular reagent.

The microbial rhodopsin sensor unit is a light-sensing protein domain discussed in photoreceptor histidine kinases. Available evidence indicates that it participates in recurring signaling strategies shared with LOV and bacteriophytochrome sensor units.

Photoreceptor-derived biosensors are engineered protein tools built from natural light-sensing photoreceptors as molecular templates. The cited review presents natural photoreceptors as a broad source for developing biosensors, fluorescent proteins, and optogenetic tools responsive to light.

Photoreceptors are naturally occurring or engineered photosensitive protein domains that respond to light at varying wavelengths and function as light-regulated actuators in optogenetics. They have been used to confer genetically encoded, light-dependent control of cellular functions, including regulation of gene expression in bacteria.

Engineered photoreceptors are protein domains used as light-sensitive actuators in microbial systems. The available evidence indicates that they function in bacterial light sensing and signal transduction and are applied in light-control strategies that modulate gene expression, protein function, and motility.

phot1 is an Arabidopsis phototropin blue-light receptor implicated in light sensing. Genetic analysis indicates that phot1 contributes to cotyledon expansion as a photomorphogenic response and, together with phot2, plays a subsidiary role in blue-light-regulated transcription.

The Light Oxygen Voltage 2 (LOV2) domain is a light-responsive protein domain from Avena sativa phototropin 1 that serves as a well-characterized foundation for the design of engineered photoswitches. The supplied evidence supports its role as a cornerstone component for optogenetic and protein-engineering applications.

Light-sensing components are natural photoreceptors found across biological kingdoms that detect light with distinct spectral properties. These proteins and domains serve as source material for engineering novel optogenetic tools.

BphP-based biosensors are proposed near-infrared optical sensor designs derived from bacterial phytochrome photoreceptors. They are suggested on the basis of bacterial phytochrome photochemistry and structure as a possible class of genetically encoded biosensors spectrally complementary to other probes.

WCC, the white collar complex, is a light-responsive heterodimeric complex in Neurospora composed of the PAS-domain-containing proteins WC-1 and WC-2. The available evidence identifies it as a major photoreceptor and suggests a role in transcriptional regulation through zinc-finger-containing subunits.

LOV-based optogenetic tools are multi-component light-responsive systems built from Light-Oxygen-Voltage sensing domains. These domains function as versatile photoreceptors involved in cellular signaling and environmental adaptation across kingdoms of life, and their continued development is intended to expand optical control of biological systems.

CcaS/R is an optimized chromatic acclimation sensor/regulator module used as a light-input induction system in a dual light-controlled co-culture platform. In the cited implementation, it operates alongside the blue light-activated YF1-FixJ-PhlF module to regulate population composition.