Source 1primary paper2017Nature Chemical Biology
Toolkit/BphP1-Q-PAS1 optogenetic pair
BphP1-Q-PAS1 optogenetic pair
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
BphP1-Q-PAS1 is a near-infrared-light-inducible optogenetic interaction pair composed of BphP1 and Q-PAS1. It enables light-controlled protein regulation, including transcription-related applications and modification of chromatin epigenetic state, and it can be combined with blue-light LOV-domain systems with negligible spectral crosstalk.
Usefulness & Problems
Why this is useful
This pair provides an optogenetic control channel in the near-infrared range that supports spectral multiplexing with blue-light systems. The reported negligible crosstalk with LOV-domain-based tools makes it useful for building multicomponent light-control schemes for protein regulation.
Source:
The BphP1-Q-PAS1 pair is a near-infrared-light-inducible interaction system. In the abstract it is used for transcription regulation, chromatin modification, and multiplexed control with blue-light systems.
Source:
near-infrared-light-inducible control of protein interactions
Source:
spectral multiplexing
Source:
chromatin epigenetic state modification
Problem solved
It addresses the need for an optogenetic interaction system that operates in a distinct spectral window and can be combined with blue-light actuators without substantial interference. The literature specifically positions Q-PAS1 as advantageous for spectral multiplexing and engineering of multicomponent systems.
Source:
It enables optogenetic control in a spectral channel that can be combined with blue-light tools while maintaining negligible crosstalk. This supports more complex multicomponent control schemes.
Source:
provides a near-infrared optogenetic pair that can be used simultaneously with blue-light tools with negligible spectral crosstalk
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.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
Use of this tool requires co-expression or provision of both BphP1 and Q-PAS1 and near-infrared illumination to induce their interaction. Reported multiplexed implementations additionally incorporate a blue-light-activatable LOV-domain-based system, and the tool is inherently a multicomponent construct architecture.
The supplied evidence is limited to a small number of reported applications and does not provide quantitative performance metrics such as kinetics, dynamic range, or binding affinity. The available text also does not establish in vivo delivery, therapeutic use, or validation beyond the reported optogenetic protein-regulation contexts.
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 source2 linked approval claimsfirst-pass slug bphp1-q-pas1-optogenetic-pair
The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state. Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk.
Source:
benchmark comparisonsupports
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.
Source:
functional applicationsupports
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.
Source:
Comparisons
Source-backed strengths
The reported BphP1-Q-PAS1 interaction is light induced and was used to modify chromatin epigenetic state, demonstrating functional control over a biologically meaningful process. In benchmarked multiplexing with a blue-light-activatable LOV-domain-based system, the pair showed negligible spectral crosstalk.
Source:
negligible spectral crosstalk with a blue-light-activatable LOV-domain-based system
Source:
supports transcription regulation and chromatin state modification
Ranked Citations
- 1.