Source 1primary paper2014ACS Synthetic Biology
Toolkit/phyB/PIF6
phyB/PIF6
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
phyB/PIF6 is a red-light-regulated optical dimerizer system composed of phyB and PIF6. In a yeast transcriptional assay, it supported light-dependent regulation and was benchmarked against phyB/PIF3, CRY2/CIB1, and TULIPs, with significant differences reported between phyB/PIF6 and phyB/PIF3 in light sensitivity and fold activation.
Usefulness & Problems
Why this is useful
This system is useful for optically controlling inducible protein interactions with red light in the context of transcriptional regulation. The available evidence specifically supports its use as one of several benchmarked optical dimerizers in yeast assays.
Source:
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
Problem solved
phyB/PIF6 helps address the problem of regulating protein-protein association with light rather than constitutive or chemically induced interactions. The cited evidence specifically places this function in a yeast transcriptional assay where light sensitivity and activation magnitude could be compared across systems.
Source:
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
Problem links
Need precise spatiotemporal control with light input
DerivedphyB/PIF6 is a red-light-regulated optical dimerizer system benchmarked as one of four inducible protein interaction tools. In a yeast transcriptional assay, it supported light-dependent regulation and differed significantly from phyB/PIF3 in light sensitivity and fold activation.
Need tighter control over gene expression timing or amplitude
DerivedphyB/PIF6 is a red-light-regulated optical dimerizer system benchmarked as one of four inducible protein interaction tools. In a yeast transcriptional assay, it supported light-dependent regulation and differed significantly from phyB/PIF3 in light sensitivity and fold activation.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Target processes
transcriptionInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
The available evidence identifies phyB/PIF6 as a multi-component optical dimerizer used in yeast transcriptional assays and regulated by red light. The supplied material does not provide construct architecture, chromophore requirements, expression details, or delivery considerations.
The supplied evidence does not report absolute activation levels, dark-state background, kinetics, reversibility, or performance outside the yeast transcriptional assay. No independent replication or application-specific demonstrations for phyB/PIF6 are provided in the supplied material.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
Approval Evidence
1 source1 linked approval claimfirst-pass slug phyb-pif6
Here, we set about to systematically benchmark the properties of four optical dimerizer systems, CRY2/CIB1, TULIPs, phyB/PIF3, and phyB/PIF6.
Source:
benchmark resultsupports
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
Source:
Comparisons
Source-backed strengths
The main demonstrated strength is that phyB/PIF6 functioned as a red-light-regulated dimerizer in a comparative benchmark study. It also exhibited significantly different light sensitivity and fold-activation behavior relative to phyB/PIF3 in a yeast transcriptional assay, indicating tunable performance within the phyB/PIF family.
Compared with iLID/SspB
phyB/PIF6 and iLID/SspB address a similar problem space because they share transcription.
Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with LITEs (Light-inducible transcriptional effectors)
phyB/PIF6 and LITEs (Light-inducible transcriptional effectors) address a similar problem space because they share transcription.
Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization; same primary input modality: light
Compared with LOVpep/ePDZb
phyB/PIF6 and LOVpep/ePDZb address a similar problem space because they share transcription.
Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
- 1.