Source 1primary paper2026MED
Toolkit/BNp-Red-1.2
BNp-Red-1.2
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
BNp-Red-1.2 is a 6 kDa protein domain from the UNICYCL system that binds the cyanobacteriochrome GAF domain NpF2164g6 to form a 1:1 complex in the dark. It serves as a compact red-light-responsive protein interaction module whose association state is coupled to the photostate of NpF2164g6.
Usefulness & Problems
Why this is useful
BNp-Red-1.2 is useful as a compact red-light-regulated interaction partner for NpF2164g6, enabling light-dependent control of protein association through a small protein module. The source positions UNICYCL as smaller and simpler than phytochrome-based red-light systems, which may reduce construct size and system complexity.
Source:
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
Problem solved
This tool helps address the need for red-light-responsive protein-protein interaction systems that are more compact and simpler than phytochrome-based platforms. The available evidence specifically supports dark-state complex formation between BNp-Red-1.2 and NpF2164g6 with micromolar affinity.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
Structural CharacterizationTarget processes
recombinationInput: Light
Implementation Constraints
Implementation requires co-use with the cyanobacteriochrome GAF domain NpF2164g6, because BNp-Red-1.2 functions through heterodimer formation with that partner. The evidence supports dark-state 1:1 complex formation with approximately 1-5 μM affinity, but does not provide additional construct design, expression, or cofactor details in the supplied material.
The supplied evidence is limited to one source and primarily documents dark-state binding and comparative positioning. No independent replication, quantitative light-state switching metrics, kinetics, spectral parameters, or application-specific validation for recombination are provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug bnp-red-1-2
Here we introduce a small red-light-only responsive system composed of a BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
Source:
binding behaviorsupports
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
Source:
light responsesupports
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
Source:
mechanistic insightsupports
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Source:
Comparisons
Source-backed strengths
BNp-Red-1.2 is very small at 6 kDa and forms a defined 1:1 complex with NpF2164g6. Reported dark-state binding occurs with an approximately 1-5 μM dissociation constant, and the associated UNICYCL platform is positioned as smaller and simpler than phytochrome-based systems.
Source:
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
Ranked Citations
- 1.