Source 1primary paper2022TSpace
Toolkit/cyanobacteriochromes
cyanobacteriochromes
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Cyanobacteriochromes are photoswitchable protein domains from cyanobacteria that sense light across a broad spectral range from the UV to the near infra-red. In the cited 2022 work, they were engineered into light-inducible dimer pairs that support orthogonal control with red, green, and blue light.
Usefulness & Problems
Why this is useful
These domains are useful as optogenetic components because their native spectral diversity enables development of multichromatic light-responsive tools. The cited study specifically positions cyanobacteriochrome-derived dimer pairs as a route to orthogonal control of biological processes with distinct visible-light inputs.
Source:
permitting orthogonal control of biological processes with red-, green-, and blue-light
Source:
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
Problem solved
This tool helps address the challenge of achieving orthogonal optogenetic control with multiple wavelengths rather than relying on a single light channel. The cited work specifically developed cyanobacteriochrome-based dimer pairs for red-, green-, and blue-light control.
Source:
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
Problem links
Need precise spatiotemporal control with light input
DerivedCyanobacteriochromes are photoswitchable protein domains from cyanobacteria that respond across a broad spectral range spanning the UV to the near infra-red. In the cited work, they were engineered into light-inducible dimer pairs that enable orthogonal control with red, green, and blue light.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
Directed EvolutionTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: actuatorswitch architecture: multi componentswitch architecture: recruitment
The available evidence indicates that the reported tools were created from cyanobacteriochrome photoswitchable proteins using directed evolution. However, the provided material does not describe construct architecture, chromophore requirements, expression conditions, or delivery considerations.
The provided evidence does not specify the individual cyanobacteriochrome variants, binding partners, kinetics, dynamic range, or host-system validation details. It also does not establish performance outside the cited study or compare these tools quantitatively to other optogenetic systems.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
The developed light inducible dimer pairs permit orthogonal control of biological processes with red-, green-, and blue-light.
permitting orthogonal control of biological processes with red-, green-, and blue-light
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
Approval Evidence
1 source2 linked approval claimsfirst-pass slug cyanobacteriochromes
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Source:
spectral rangesupports
Cyanobacteriochromes respond to a wide range of wavelengths from the UV to the near infra-red.
Cyanobacteriochromes, photoswitchable proteins from cyanobacteria, respond to a wide range of wavelengths from the UV to the near infra-red.
Source:
tool developmentsupports
New light inducible dimer pairs were developed from cyanobacteriochrome photoswitchable proteins via directed evolution approaches.
New light inducible dimer pairs from these photoswitchable proteins are developed via directed evolution approaches
Source:
Comparisons
Source-backed strengths
A key strength is the broad underlying spectral responsiveness of cyanobacteriochromes, spanning UV to near infra-red. The cited work further reports development of new light-inducible dimer pairs and states that these permit orthogonal control with red, green, and blue light.
Compared with light-oxygen-voltage sensing (LOV) domain
cyanobacteriochromes and light-oxygen-voltage sensing (LOV) domain address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: light
Compared with optogenetic RGS2
cyanobacteriochromes and optogenetic RGS2 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: light
Compared with split-TurboID
cyanobacteriochromes and split-TurboID address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
- 1.