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.
Source:
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.
Source:
near-infrared-light-inducible protein regulation
Source:
spectral multiplexing with blue-light tools
Source:
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.
Source:
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.
Source:
reduces size and oligomerization limitations of the PpsR2 partner in the BphP1-PpsR2 system
Problem links
reduces size and oligomerization limitations of the PpsR2 partner in the BphP1-PpsR2 system
LiteratureIt 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.
Source:
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.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
HeterodimerizationHeterodimerizationHeterodimerizationOligomerizationoligomerization suppressionTechniques
No technique tags yet.
Target processes
transcriptionImplementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenlight modality: near-infraredoperating role: regulatorsingle domain: Trueswitch architecture: multi componentswitch architecture: recruitment
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.
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.
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 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 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 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
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
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
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.
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.
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
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
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
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.
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.
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.
Source:
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.
Source:
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.
Source:
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-stated alternatives
The abstract contrasts Q-PAS1 with the natural PpsR2 partner and with blue-light-activatable LOV-domain-based systems used in combination for multiplexing.
Source:
The abstract contrasts Q-PAS1 with the natural PpsR2 partner and with blue-light-activatable LOV-domain-based systems used in combination for multiplexing.
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.
Source:
three-fold smaller than PpsR2
Source:
lacks oligomerization
Source:
supports negligible spectral crosstalk with a blue-light-activatable LOV-domain-based system
Compared with basic helix-loop-helix (bHLH) domain
Q-PAS1 and basic helix-loop-helix (bHLH) domain address a similar problem space because they share transcription.
Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization
Compared with CIB1
Q-PAS1 and CIB1 address a similar problem space because they share transcription.
Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization, oligomerization
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with Enhanced Magnets
Q-PAS1 and Enhanced Magnets address a similar problem space because they share transcription.
Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization
Relative tradeoffs: appears more independently replicated.
Ranked Citations
- 1.