Source 1primary paper2023
Toolkit/Enhanced Magnets
Enhanced Magnets
Also known as: eMags
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Enhanced Magnets (eMags) are Vivid-derived light-sensitive protein dimerization domains used in optogenetic split transcription factors and subcellular recruitment systems. In Saccharomyces cerevisiae, optimized eMag-based transcription factor designs improved light-sensitive gene expression, and eMags were also validated for rapid, reversible protein recruitment to subcellular organelles.
Usefulness & Problems
Why this is useful
eMags provide a genetically encoded light-controlled interaction module for regulating transcription and recruiting proteins to defined subcellular locations. The available evidence indicates utility both in yeast optogenetic toolkit development and in subcellular optogenetics requiring rapid and reversible control.
Source:
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Source:
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
Source:
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Source:
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
Problem solved
eMags help solve the problem of controlling protein association with light in a modular format that can be inserted into split transcription factors or recruitment constructs. The cited work specifically addresses improved light-sensitive gene expression in Saccharomyces cerevisiae and reversible organelle-localized protein recruitment.
Source:
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
Problem links
Need precise spatiotemporal control with light input
DerivedEnhanced Magnets (eMags) are light-sensitive dimerizing protein domains derived from Vivid-based Magnets and incorporated into optogenetic split transcription factors. In Saccharomyces cerevisiae, optimized eMag-based transcription factor designs supported improved light-sensitive gene expression, and the domains were also validated for rapid, reversible protein recruitment to subcellular organelles.
Need tighter control over gene expression timing or amplitude
DerivedEnhanced Magnets (eMags) are light-sensitive dimerizing protein domains derived from Vivid-based Magnets and incorporated into optogenetic split transcription factors. In Saccharomyces cerevisiae, optimized eMag-based transcription factor designs supported improved light-sensitive gene expression, and the domains were also validated for rapid, reversible protein recruitment to subcellular organelles.
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
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: actuatoroperating role: regulatorswitch architecture: multi componentswitch architecture: recruitmentswitch architecture: split
eMags have been integrated into split transcription factors in Saccharomyces cerevisiae and into constructs for protein recruitment to subcellular organelles. The evidence supports use within modular cloning and high-throughput characterization workflows, but it does not specify cofactors, expression constraints, or detailed construct architecture.
The supplied evidence does not report quantitative performance metrics, illumination wavelengths, dynamic range, kinetics, or comparisons against alternative dimerizers beyond noting improvement after optimization. Validation is described in yeast transcription-factor contexts and subcellular recruitment, so broader organismal and application scope is not established here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2020
Ranked Claims
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Laboratory automation combined with a modular cloning scheme enables high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae.
We combine laboratory automation and a modular cloning scheme to enable high-throughput construction and characterization of optogenetic split transcription factors in Saccharomyces cerevisiae .
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
An optimized Enhanced Magnet transcription factor showed improved light-sensitive gene expression.
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
Approval Evidence
2 sources5 linked approval claimsfirst-pass slug enhanced-magnets
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
Source:
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles
Source:
design integrationsupports
Cryptochrome and Enhanced Magnet light-sensitive dimerizers were incorporated into split transcription factors.
incorporate these light-sensitive dimerizers into split transcription factors
Source:
toolkit expansionsupports
The yeast optogenetic toolkit was expanded to include variants of cryptochromes and Enhanced Magnets.
We expand the yeast optogenetic toolkit to include variants of the cryptochromes and Enhanced Magnets
Source:
application capabilitysupports
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
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engineering improvementsupports
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
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utility statementsupports
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
Source:
Comparisons
Source-backed strengths
The reported strengths are improved light-sensitive gene expression in an optimized eMag split transcription factor and validation for rapid, reversible recruitment to subcellular organelles. eMags were also incorporated into a modular, high-throughput yeast optogenetics workflow, supporting scalable construction and characterization of designs.
Source:
We use this approach to rationally design and test an optimized Enhanced Magnet transcription factor with improved light-sensitive gene expression.
Source:
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
Compared with CIB1 N-terminal CRY2-binding region
Enhanced Magnets and CIB1 N-terminal CRY2-binding region 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
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with cryptochromes
Enhanced Magnets and cryptochromes 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 TAEL
Enhanced Magnets and TAEL 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
Ranked Citations
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