Source 1primary paper2026MED
Toolkit/UNICYCL
UNICYCL
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
UNICYCL is a red-light-regulated multi-component protein interaction switch built from the cyanobacteriochrome NpF2164g6 and the binder BNp-Red-1.2. In the dark, BNp-Red-1.2 forms a 1:1 complex with NpF2164g6 with an approximately 1–5 μM dissociation constant, enabling reversible light-controlled association.
Usefulness & Problems
Why this is useful
UNICYCL is useful as a red-light-responsive protein interaction module for controlling processes that can be coupled to regulated complex formation. The available evidence positions it as a smaller and simpler alternative to phytochrome-based red-light systems.
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
UNICYCL addresses the need for a red-light-controlled protein-protein interaction switch that is more compact and simpler than phytochrome-based tools. The supplied evidence supports its use as a reversible association module based on NpF2164g6 and BNp-Red-1.2.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
Structural CharacterizationTarget processes
recombinationInput: Light
Implementation Constraints
UNICYCL is implemented as a two-component system comprising NpF2164g6 and the binder BNp-Red-1.2. The supplied evidence does not provide additional practical details on cofactors, construct architecture, expression context, or delivery.
The supplied evidence is limited to one source and provides little quantitative information beyond dark-state affinity and complex stoichiometry. The evidence provided here does not include detailed performance data for switching contrast, kinetics under illumination, cellular validation, or recombination-specific outcomes.
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 source4 linked approval claimsfirst-pass slug unicycl
Red-Light-Only Control of Protein-Protein Interactions Using a Cyanobacteriochrome (UNICYCL).
Source:
comparative positioningsupports
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...
Source:
kinetic propertysupports
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.
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:
tool capabilitysupports
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.
Source:
Comparisons
Source-backed strengths
The reported dark-state interaction between BNp-Red-1.2 and NpF2164g6 has an approximately 1–5 μM dissociation constant and a defined 1:1 stoichiometry. The source literature also positions UNICYCL as comparatively smaller and simpler than phytochrome-based red-light 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.