Source 1primary paper2017Nature Chemical Biology
Toolkit/Q-PAS1
Q-PAS1
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Q-PAS1 is an engineered single-domain binding partner for the bacterial phytochrome BphP1 that enables near-infrared-light-inducible protein interactions. It was developed as a smaller, non-oligomerizing alternative to the natural BphP1 partner PpsR2 and has been applied to transcription regulation, chromatin state modification, and spectral multiplexing.
Usefulness & Problems
Why this is useful
Q-PAS1 is useful as a compact interaction module for near-infrared optogenetics in systems where the natural PpsR2 partner is limited by larger size, multidomain architecture, and oligomeric behavior. The reported negligible spectral crosstalk with a blue-light LOV-based system also makes it useful for multiplexed and multicomponent optical control.
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Q-PAS1 is an engineered single-domain binding partner for BphP1 that enables near-infrared-light-inducible interactions. The abstract describes its use in transcription regulation, chromatin state modification, and multiplexed optogenetic control.
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near-infrared-light-inducible protein regulation
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spectral multiplexing with blue-light tools
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engineering multicomponent optogenetic systems
Problem solved
Q-PAS1 addresses the engineering limitations of the natural BphP1 partner PpsR2 by providing a single-domain binder that is three-fold smaller and lacks oligomerization. This specifically helps enable near-infrared-inducible regulation in applications such as transcription control and chromatin state modification while improving compatibility with spectral multiplexing.
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It addresses the large size, multidomain structure, and oligomeric behavior that limited use of the natural PpsR2 partner. The smaller non-oligomerizing design is presented as better suited for multiplexing and multicomponent engineering.
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reduces size and oligomerization limitations of the PpsR2 partner in the BphP1-PpsR2 system
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
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
transcriptionImplementation Constraints
Q-PAS1 is used together with BphP1 as a near-infrared optogenetic interaction pair. Reported applications include transcription regulation and chromatin state modification, and some implementations combine the pair with a blue-light LOV-domain-based system for spectral multiplexing.
The supplied evidence is limited to a single cited study and brief extraction text, so quantitative performance metrics, binding properties, and generality across organisms or cell types are not established here. The evidence also does not define whether Q-PAS1 alone is sufficient for broader optogenetic applications beyond the reported near-infrared interaction, transcription regulation, chromatin state modification, and multiplexing use cases.
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 source3 linked approval claimsfirst-pass slug q-pas1
Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization.
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comparative advantagesupports
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.
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engineering outcomesupports
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.
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functional applicationsupports
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.
Source:
Comparisons
Source-backed strengths
The source states that Q-PAS1 is three-fold smaller than the natural partner and lacks oligomerization, which are direct engineering advantages for construct design and multicomponent systems. In the cited study, the BphP1-Q-PAS1 pair showed negligible spectral crosstalk when multiplexed with a blue-light-activatable LOV-domain-based system, and Q-PAS1 was described as superior for spectral multiplexing and engineering of multicomponent systems.
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three-fold smaller than PpsR2
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lacks oligomerization
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supports negligible spectral crosstalk with a blue-light-activatable LOV-domain-based system
Ranked Citations
- 1.