Source 1review2020Current Opinion in Cell Biology
Toolkit/PhoCl
PhoCl
Also known as: photocleavable protein
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
PhoCl is a light-responsive protein domain that cleaves upon 405 nm illumination. In the SPLIT system, it was fused between maltose-binding protein and a tandem RGG coacervation module to trigger light-induced assembly of synthetic membraneless organelles in Saccharomyces cerevisiae after a single light pulse.
Usefulness & Problems
Why this is useful
PhoCl is useful as an optogenetic trigger for irreversible protein-state changes because its light response is encoded directly in a protein domain that undergoes cleavage. In the cited application, this enabled single-pulse control over coacervation and the formation of tunable synthetic membraneless organelles.
Source:
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
Source:
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Problem solved
This tool helps solve the problem of how to convert a brief light input into assembly of a coacervating protein system. In the reported design, PhoCl-mediated cleavage removed a solubilizing constraint from a fusion protein, enabling RGG-driven coacervation in yeast.
Source:
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
Problem links
Need precise spatiotemporal control with light input
DerivedPhoCl is a light-responsive protein domain that undergoes cleavage upon 405 nm illumination. In the cited SPLIT system, PhoCl was used within a fusion protein to remove a solubilizing domain and thereby trigger RGG-driven coacervation after a single light pulse.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuatorswitch architecture: cleavageswitch architecture: split
In the cited construct, PhoCl was incorporated into a fusion protein containing a solubilizing maltose-binding protein domain and two copies of an RGG domain. Activation was achieved with 405 nm light, and the demonstrated application was in Saccharomyces cerevisiae.
The supplied evidence supports PhoCl only in the context of the SPLIT fusion construct and does not provide standalone performance metrics such as cleavage efficiency, kinetics, dynamic range, or phototoxicity. Validation in the provided evidence is limited to a yeast coacervation application.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2020ACS Synthetic Biology
Source 3review2021Advanced Biology
Ranked Claims
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of the system displayed light-induced coacervation in Saccharomyces cerevisiae.
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
The authors engineered a coacervating protein to create tunable synthetic membraneless organelles that assemble in response to a single pulse of light.
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
coacervation time within minutesillumination duration several secondsillumination wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
activation wavelength 405 nm
Approval Evidence
3 sources3 linked approval claimsfirst-pass slug phocl
The web research summary states that the review explicitly discusses PhoCl as a photocleavable protein and a tool/component in the anchor review.
Source:
web_research_summary lists PhoCl as an explicitly supported tool mentioned in the anchor review and describes it as a photocleavable optogenetic protein for controlling localization and enzyme activity
Source:
opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light
Source:
construct compositionsupports
The fusion protein contains a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
We developed a fusion protein containing a solubilizing maltose-binding protein domain, PhoCl, and two copies of the RGG domain.
Source:
functional performancesupports
Several seconds of 405 nm illumination is sufficient to cleave PhoCl, remove the solubilization domain, and enable RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Several seconds of illumination at 405 nm is sufficient to cleave PhoCl, removing the solubilization domain and enabling RGG-driven coacervation within minutes in cellular-sized water-in-oil emulsions.
Source:
mechanismsupports
In the reported system, coacervation is driven by the LAF-1 RGG domain and light responsiveness is provided by PhoCl cleavage in response to 405 nm light.
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1, and opto-responsiveness is coded by the protein PhoCl, which cleaves in response to 405 nm light.
Source:
Comparisons
Source-backed strengths
The cited study reports that an optimized system displayed light-induced coacervation in Saccharomyces cerevisiae. The response was triggered by a single 405 nm light pulse, supporting its use for temporally precise induction of synthetic membraneless organelle assembly.
Source:
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
Compared with AsLOV2-Jα
PhoCl and AsLOV2-Jα address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: photocleavage; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with light-harvesting complex II
PhoCl and light-harvesting complex II address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: photocleavage; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with RGG domain from LAF-1
PhoCl and RGG domain from LAF-1 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: photocleavage; same primary input modality: light
Ranked Citations
- 1.
Extracted from this source document.
- 2.
- 3.
Extracted from this source document.