Source 1primary paper2017Nature Chemical Biology
Toolkit/Q-PAS1-LOV integrated optogenetic tool
Q-PAS1-LOV integrated optogenetic tool
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Q-PAS1-LOV integrated optogenetic tool is a dual-color, multi-component optogenetic system that combines Q-PAS1 with a blue-light-activatable LOV-domain-based module in a single platform. It enables tridirectional protein targeting with independent control by near-infrared and blue light.
Usefulness & Problems
Why this is useful
This tool is useful for spectral multiplexing because it supports independent regulation by near-infrared and blue light with negligible spectral crosstalk. The source literature also states that Q-PAS1 is superior for spectral multiplexing and for engineering multicomponent systems.
Source:
This integrated optogenetic tool combines Q-PAS1 and LOV domains in one system. The abstract states that it enables tridirectional protein targeting under independent near-infrared and blue light control.
Source:
tridirectional protein targeting
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independent control by near-infrared and blue light
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multicomponent optogenetic engineering
Problem solved
This system addresses the need for more complex optical control than a single photoswitch can provide by enabling independent dual-wavelength regulation within one optogenetic platform. Specifically, it supports tridirectional protein targeting under separate near-infrared and blue light inputs.
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It supports more complex multicomponent control than a single light-responsive module alone by enabling independent dual-color regulation.
Source:
enables integrated multichannel light control within a single optogenetic tool
Published Workflows
Objective: Engineer an improved near-infrared optogenetic interaction partner for BphP1 and use it to build multiplexable protein regulation systems with low spectral crosstalk.
Why it works: The abstract presents Q-PAS1 as a smaller, non-oligomerizing BphP1 partner that overcomes limitations of PpsR2, which is expected to improve compatibility with multiplexed and multicomponent optogenetic designs.
light-induced BphP1-Q-PAS1 bindingindependent near-infrared and blue light controlprotein engineeringoptogenetic system integrationspectral multiplexing
Stages
- 1.Engineering of an improved BphP1 binding partner(library_design)
The natural PpsR2 partner limited applications because of large size, multidomain structure, and oligomeric behavior.
Selection: Create a single-domain BphP1 binding partner that is smaller and lacks oligomerization relative to PpsR2.
- 2.Functional development of transcription regulation systems(functional_characterization)
To demonstrate that the engineered partner can support practical optogenetic regulation functions.
Selection: Use the helix-PAS fold of Q-PAS1 to build near-infrared-light-controllable transcription regulation systems.
- 3.Application to chromatin epigenetic state modification(secondary_characterization)
To extend validation beyond transcription regulation to chromatin-level control.
Selection: Test whether light-induced BphP1-Q-PAS1 interaction can modify chromatin epigenetic state.
- 4.Spectral multiplexing test with blue-light system(confirmatory_validation)
To confirm that the near-infrared pair can be used simultaneously with blue-light tools.
Selection: Assess spectral crosstalk when combining the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system.
- 5.Integration into a single dual-color optogenetic tool(confirmatory_validation)
To demonstrate utility of Q-PAS1 in a more complex multicomponent engineered system.
Selection: Integrate Q-PAS1 and LOV domains in one tool and test for tridirectional protein targeting under independent near-infrared and blue light control.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
independent dual-wavelength controllight-controlled protein targetingspectral multiplexingTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
Implementation requires integration of Q-PAS1 and LOV domains within a single optogenetic tool context and operation with both near-infrared and blue light. The supplied evidence does not provide details on cofactors, host organisms, expression systems, or construct design beyond this domain integration.
The available evidence is limited to the reported targeting behavior and comparative statements about multiplexing performance. The source text does not specify quantitative performance metrics, construct architecture, delivery strategy, expression context, or validation across multiple biological systems.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system showed negligible spectral crosstalk.
Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is superior for spectral multiplexing and engineering of multicomponent systems.
thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Q-PAS1 is an engineered single-domain BphP1 binding partner that is three-fold smaller than PpsR2 and lacks oligomerization.
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
size reduction versus PpsR2 three-fold smaller
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
Q-PAS1 was used to develop near-infrared-light-controllable transcription regulation systems enabling either 40-fold activation or inhibition.
We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition.
transcription regulation effect 40-fold activation or inhibition
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state.
Approval Evidence
1 source1 linked approval claimfirst-pass slug q-pas1-lov-integrated-optogenetic-tool
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Source:
functional applicationsupports
Integrating Q-PAS1 and LOV domains in a single optogenetic tool enabled tridirectional protein targeting independently controlled by near-infrared and blue light.
By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light.
Source:
Comparisons
Source-backed strengths
The reported strengths are independent control by near-infrared and blue light and negligible spectral crosstalk when multiplexed with a blue-light-activatable LOV-domain-based system. The literature further identifies Q-PAS1 as advantageous for spectral multiplexing and multicomponent system engineering.
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supports tridirectional protein targeting
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independently controlled by near-infrared and blue light
Ranked Citations
- 1.