Source 1primary paper2020
Toolkit/optogenetic switch for Set2 methyltransferase
optogenetic switch for Set2 methyltransferase
Also known as: rapid and reversible optogenetic control for Set2
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
This tool is a rapid and reversible optogenetic switch for the yeast Set2 methyltransferase generated by fusing Set2, the sole H3K36 methyltransferase in yeast, to the light-activated nuclear shuttle (LANS) domain. It uses light to control Set2 subcellular localization and was applied to interrogate in vivo H3K36me2 and H3K36me3 dynamics.
Usefulness & Problems
Why this is useful
The switch enables temporal control of Set2 activity in living yeast through light-controlled nuclear shuttling, allowing dynamic perturbation of H3K36 methylation without permanent genetic removal of the enzyme. In the cited study, it was used to reveal rapid H3K36me3 accumulation, correlation of total H3K36me3 with RNA abundance, and rapid H3K36me2/3 removal that depended strongly on the demethylase Rph1.
Source:
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
Problem solved
This tool addresses the problem of probing the kinetics of H3K36 methylation and demethylation in vivo with rapid and reversible control over the sole H3K36 methyltransferase in yeast. It specifically enables dissection of transcription-dependent and transcription-independent dynamics of H3K36me2/3 deposition and removal.
Problem links
Need precise spatiotemporal control with light input
DerivedThis tool is an optogenetic switch for the yeast Set2 methyltransferase created by fusing Set2 to the light-activated nuclear shuttle (LANS) domain. It enables rapid and reversible light control of the sole H3K36 methyltransferase in yeast and was used to probe in vivo H3K36me2/3 dynamics.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
light-controlled nuclear shuttlinglight-controlled nuclear shuttlingoptogenetic subcellular relocalizationoptogenetic subcellular relocalizationTechniques
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: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: actuatorswitch architecture: multi component
The construct was created by domain fusion of Set2 to the light-activated nuclear shuttle (LANS) domain. The available evidence supports implementation in yeast and indicates that light is the input modality controlling Set2 nuclear shuttling, but it does not specify wavelengths, expression strategy, or additional construct architecture details.
The supplied evidence is limited to a single 2020 study and does not provide quantitative performance metrics such as switching speed, dynamic range, leakiness, or illumination parameters. Evidence for use is confined to yeast Set2 and H3K36 methylation dynamics, with no independent replication or cross-system validation provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
Approval Evidence
1 source5 linked approval claimsfirst-pass slug optogenetic-switch-for-set2-methyltransferase
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
Source:
demethylation observationsupports
Removal of H3K36me2/3 was rapid and highly dependent on the demethylase Rph1.
Removal H3K36me2/3 was also rapid and highly dependent on the demethylase Rph1.
Source:
dynamic observationsupports
Early H3K36me3 dynamics showed rapid methylation in vivo, and total H3K36me3 levels correlated with RNA abundance.
Early H3K36me3 dynamics identified rapid methylation in vivo , with total H3K36me3 levels correlating with RNA abundance.
Source:
kinetic patternsupports
Across genes, relative rates of H3K36me3 accumulation were largely linear and consistent, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Although genes exhibited disparate levels of H3K36 methylation, relative rates of H3K36me3 accumulation were largely linear and consistent across genes, suggesting a rate-limiting mechanism for H3K36me3 deposition.
Source:
kinetic patternsupports
The per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting that H3K36 demethylases act in a global, stochastic manner.
However, the per-gene rate of H3K36me3 loss weakly correlated with RNA abundance and followed exponential decay, suggesting H3K36 demethylases act in a global, stochastic manner.
Source:
tool establishmentsupports
The authors established rapid and reversible optogenetic control of the yeast Set2 methyltransferase by fusing Set2 to the LANS domain.
We established rapid and reversible optogenetic control for Set2, the sole H3K36 methyltransferase in yeast, by fusing the enzyme with the light activated nuclear shuttle (LANS) domain.
Source:
Comparisons
Source-backed strengths
The reported design provides rapid and reversible optogenetic control of Set2 in yeast. Its application produced kinetic observations across genes, including largely linear and consistent relative rates of H3K36me3 accumulation, supporting its utility for time-resolved chromatin regulation studies.
Compared with ArrayG
optogenetic switch for Set2 methyltransferase and ArrayG address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Compared with GFP-PHR-caspase8/Flag-CIB1N-caspase8
optogenetic switch for Set2 methyltransferase and GFP-PHR-caspase8/Flag-CIB1N-caspase8 address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Compared with light-switchable transcription factors
optogenetic switch for Set2 methyltransferase and light-switchable transcription factors address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Ranked Citations
- 1.