Source 1primary paper2012Proteins Structure Function and Bioinformatics
Toolkit/LOV-TAP
LOV-TAP
Also known as: light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP)
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
LOV-TAP is an artificial light-activable allosteric protein constructed by ligating the AsLOV2-Jα photoswitch to the tryptophan repressor TrpR. It is designed to regulate protein-DNA association by coupling light-triggered changes in the LOV module to structural and electrostatic changes in the interdomain region that alter DNA binding.
Usefulness & Problems
Why this is useful
LOV-TAP is useful as a genetically encoded light-responsive switch for controlling DNA binding with a LOV-based photosensory input. The cited study specifically supports its value for probing how photoinduced structural and electrostatic changes can regulate protein-DNA association.
Problem solved
LOV-TAP addresses the problem of making DNA binding responsive to light by fusing a photoswitchable LOV domain to a DNA-binding protein. The available evidence indicates that it was developed to control TrpR-associated DNA binding through photoinduced allosteric regulation.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
allosteric switchingelectrostatic modulation of protein-dna associationjα-helix undocking/cleavage from the lov corelight-induced covalent cys450-fmn adduct formationlight-regulated dna bindingPhotocleavageTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
LOV-TAP consists of a domain fusion between AsLOV2-Jα and TrpR, and its function depends on the LOV chromophore FMN and the reactive Cys450 residue that forms the light-induced adduct. Beyond this composition and photochemical requirement, the supplied evidence does not describe construct architecture details, host systems, delivery methods, or assay conditions.
The supplied evidence comes from a single 2012 computer simulation study, so support is mechanistic and computational rather than broad experimental validation. No quantitative performance metrics, illumination parameters, expression context, or independent replication are provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Approval Evidence
1 source5 linked approval claimsfirst-pass slug lov-tap
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP)
Source:
compositionsupports
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
Source:
mechanismsupports
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
Source:
mechanismsupports
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
Source:
mechanismsupports
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Source:
mechanismsupports
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Source:
Comparisons
Source-backed strengths
The reported mechanism links a defined photochemical event, Cys450-FMN adduct formation in AsLOV2-Jα, to Jα-helix cleavage from the LOV core and subsequent changes in DNA association. The study further proposes a coherent mechanistic model in which light increases LOV-TAP polarity, promotes electrostatic attraction to DNA, and enables condensation onto the DNA surface through unfolding and flexibilization of a hairpin-like interdomain region.
Ranked Citations
- 1.