Source 1primary paper2020ACS Synthetic Biology
Toolkit/RGG domain from LAF-1
RGG domain from LAF-1
Also known as: RGG domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The RGG domain from LAF-1 is an intrinsically disordered coacervation-driving module used in a light-triggered synthetic condensate system. In the reported SPLIT construct, two LAF-1 RGG domains are fused with PhoCl and a maltose-binding protein solubilization domain to form tunable synthetic membraneless organelles after a single light pulse.
Usefulness & Problems
Why this is useful
This domain is useful as the phase-separation module in engineered systems that create synthetic membraneless organelles on demand. In the cited SPLIT design, it enables light-induced coacervation and stable assembly of condensates in Saccharomyces cerevisiae.
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
It helps solve the problem of triggering intracellular condensate assembly with temporal control using light rather than constitutive coacervation. The reported system was engineered to generate tunable synthetic membraneless organelles in response to a single pulse of light.
Source:
An optimized version of this system displayed light-induced coacervation in Saccharomyces cerevisiae.
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
In the reported construct, coacervation is driven by two copies of the intrinsically disordered LAF-1 RGG domain fused to PhoCl and a solubilizing maltose-binding protein domain. The validated application was in Saccharomyces cerevisiae, where an optimized version showed light-induced coacervation.
The evidence here is limited to one reported SPLIT implementation and does not isolate the RGG domain as a standalone optogenetic tool. Quantitative performance metrics, generality across organisms or cargos, and detailed photophysical operating parameters are not provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
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.
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.
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
Approval Evidence
1 source3 linked approval claimsfirst-pass slug rgg-domain-from-laf-1
Coacervation is driven by the intrinsically disordered RGG domain from the protein LAF-1
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 available evidence shows that the LAF-1 RGG domain can drive coacervation when incorporated into an optimized light-responsive fusion protein. The system was validated in Saccharomyces cerevisiae and was reported to assemble tunable synthetic membraneless organelles after light exposure.
Source:
We have engineered a coacervating protein to create tunable, synthetic membraneless organelles that assemble in response to a single pulse of light.
Ranked Citations
- 1.