Source 1primary paper2023Nucleic Acids Research
Toolkit/GntR
GntR
Also known as: gluconate-responsive transcriptional repressor GntR
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
GntR is a gluconate-responsive transcriptional repressor from Escherichia coli that has been repurposed as a protein domain for synthetic gene-control switches. Reported designs use GntR to construct gluconate-regulated transcriptional systems in mammalian cells, including rewired OFF/ON transcriptional architectures and a split transcriptional activator.
Usefulness & Problems
Why this is useful
GntR is useful as a small-molecule-responsive regulatory domain for controlling transgene expression with gluconate. The cited work specifically positions it as a basis for mammalian gene switches responsive to a clinically licensed inducer.
Problem solved
This tool helps solve the problem of building mammalian transcription systems that respond to gluconate rather than relying on GntR's native bacterial regulatory context. It enables synthetic OFF- and ON-type control by rewiring gluconate-dependent DNA binding or by exploiting GntR dimerization in a split activator design.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Target processes
recombinationselectiontranscriptionImplementation Constraints
The source evidence identifies GntR as originating from Escherichia coli and being used in mammalian-cell switch designs. Practical construct details such as promoter architecture, operator sequence design, expression format, delivery method, and gluconate dosing are not provided in the supplied evidence.
The supplied evidence is limited to a single 2023 study and does not provide quantitative performance metrics, dynamic range, leakiness, response kinetics, or cross-context validation. The evidence also does not establish use in processes beyond transcription, despite broader target-process labels in the input.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
A gluconate-responsive switch was built by using GntR dimerization in the presence of gluconate to activate gene expression from a split transcriptional activator.
Then, we utilized the ability of GntR to dimerize in the presence of gluconate to activate gene expression from a split transcriptional activator.
A gluconate-responsive switch was built by using GntR dimerization in the presence of gluconate to activate gene expression from a split transcriptional activator.
Then, we utilized the ability of GntR to dimerize in the presence of gluconate to activate gene expression from a split transcriptional activator.
A gluconate-responsive switch was built by using GntR dimerization in the presence of gluconate to activate gene expression from a split transcriptional activator.
Then, we utilized the ability of GntR to dimerize in the presence of gluconate to activate gene expression from a split transcriptional activator.
A gluconate-responsive switch was built by using GntR dimerization in the presence of gluconate to activate gene expression from a split transcriptional activator.
Then, we utilized the ability of GntR to dimerize in the presence of gluconate to activate gene expression from a split transcriptional activator.
A gluconate-responsive switch was built by using GntR dimerization in the presence of gluconate to activate gene expression from a split transcriptional activator.
Then, we utilized the ability of GntR to dimerize in the presence of gluconate to activate gene expression from a split transcriptional activator.
A gluconate-responsive switch was built by using GntR dimerization in the presence of gluconate to activate gene expression from a split transcriptional activator.
Then, we utilized the ability of GntR to dimerize in the presence of gluconate to activate gene expression from a split transcriptional activator.
A gluconate-responsive switch was built by using GntR dimerization in the presence of gluconate to activate gene expression from a split transcriptional activator.
Then, we utilized the ability of GntR to dimerize in the presence of gluconate to activate gene expression from a split transcriptional activator.
OFF- and ON-type switches were assembled by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Initially we assembled OFF- and ON-type switches by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
OFF- and ON-type switches were assembled by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Initially we assembled OFF- and ON-type switches by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
OFF- and ON-type switches were assembled by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Initially we assembled OFF- and ON-type switches by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
OFF- and ON-type switches were assembled by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Initially we assembled OFF- and ON-type switches by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
OFF- and ON-type switches were assembled by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Initially we assembled OFF- and ON-type switches by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
OFF- and ON-type switches were assembled by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Initially we assembled OFF- and ON-type switches by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
OFF- and ON-type switches were assembled by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Initially we assembled OFF- and ON-type switches by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Random mutagenesis of GntR combined with phenotypic screening identified variants that significantly enhanced the functionality of the genetic devices.
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Random mutagenesis of GntR combined with phenotypic screening identified variants that significantly enhanced the functionality of the genetic devices.
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Random mutagenesis of GntR combined with phenotypic screening identified variants that significantly enhanced the functionality of the genetic devices.
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Random mutagenesis of GntR combined with phenotypic screening identified variants that significantly enhanced the functionality of the genetic devices.
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Random mutagenesis of GntR combined with phenotypic screening identified variants that significantly enhanced the functionality of the genetic devices.
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Random mutagenesis of GntR combined with phenotypic screening identified variants that significantly enhanced the functionality of the genetic devices.
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Random mutagenesis of GntR combined with phenotypic screening identified variants that significantly enhanced the functionality of the genetic devices.
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Approval Evidence
1 source4 linked approval claimsfirst-pass slug gntr
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Source:
design basissupports
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Several switch designs were assembled based on the gluconate-responsive transcriptional repressor GntR from Escherichia coli.
Source:
mechanism designsupports
A gluconate-responsive switch was built by using GntR dimerization in the presence of gluconate to activate gene expression from a split transcriptional activator.
Then, we utilized the ability of GntR to dimerize in the presence of gluconate to activate gene expression from a split transcriptional activator.
Source:
mechanism designsupports
OFF- and ON-type switches were assembled by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Initially we assembled OFF- and ON-type switches by rewiring the native gluconate-dependent binding of GntR to target DNA sequences in mammalian cells.
Source:
optimization resultsupports
Random mutagenesis of GntR combined with phenotypic screening identified variants that significantly enhanced the functionality of the genetic devices.
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Source:
Comparisons
Source-backed strengths
The reported strength of GntR is its versatility across multiple switch architectures assembled from the same gluconate-responsive bacterial regulator. Evidence supports both DNA-binding-rewired OFF/ON systems in mammalian cells and a dimerization-based split transcriptional activator responsive to gluconate.
Source:
By means of random mutagenesis of GntR combined with phenotypic screening, we identified variants that significantly enhanced the functionality of the genetic devices
Ranked Citations
- 1.