Toolkit/LOV2 domain from Avena sativa phototropin1

LOV2 domain from Avena sativa phototropin1

Protein Domain·Research·Since 2012

Also known as: light-sensitive LOV2 domain

Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

The LOV2 domain from Avena sativa phototropin1 is a blue-light-responsive sensory domain that was fused to the restriction endonuclease PvuII to create a genetically encoded light-controllable chimeric nuclease. In this context, LOV2 modulates DNA cleavage activity in response to blue light, with the direction of regulation determined by the fusion interface.

Usefulness & Problems

Why this is useful

This domain is useful as a modular photosensory element for engineering light control over enzyme function through genetic fusion. In the reported PvuII chimera, it enabled optical regulation of nuclease activity, providing a route to externally control DNA cleavage with blue light.

Problem solved

It addresses the problem of making restriction endonuclease activity controllable by a noninvasive external input. Specifically, fusion of LOV2 to PvuII produced a nuclease whose DNA cleavage activity differed between dark and blue-light conditions.

Problem links

Need precise spatiotemporal control with light input

Derived

The LOV2 domain from Avena sativa phototropin1 was fused to the restriction endonuclease PvuII to create a genetically encoded light-controllable chimeric nuclease. In this configuration, blue light modulates DNA cleavage activity, and the direction of regulation depends on the fusion interface.

Taxonomy & Function

Primary hierarchy

Mechanism Branch

Component: A low-level protein part used inside a larger architecture that realizes a mechanism.

Techniques

No technique tags yet.

Target processes

No target processes tagged yet.

Input: Light

Implementation Constraints

cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuatorswitch architecture: uncaging

The demonstrated implementation used domain fusion between the Avena sativa phototropin1 LOV2 domain and the restriction enzyme PvuII. Functional behavior depended on the fusion interface, indicating that construct architecture is a critical design parameter for determining whether activity is favored in the dark or under blue light.

The supplied evidence is limited to a single reported fusion context with PvuII and does not establish general performance across other target proteins or organisms. The observed activity modulation was reported as 3-fold, and no broader validation, in vivo deployment details, or comparative benchmarking are provided here.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 2activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 3activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 4activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 5activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 6activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 7activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 8activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 9activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 10activity modulationsupports2012Source 1needs review

Analyzed LOV-PvuII fusion variants showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions.

By analyzing several LOV-PvuII fusion enzymes, variants were obtained that show a 3-fold difference in DNA cleavage activity, when illuminated with blue light or kept in the dark.
DNA cleavage activity difference 3 fold
Claim 11engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 12engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 13engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 14engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 15engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 16engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 17engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 18engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 19engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 20engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 21engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 22engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 23engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 24engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 25engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 26engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 27engineering resultsupports2012Source 1needs review

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.
Claim 28mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 29mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 30mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 31mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 32mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 33mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 34mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 35mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 36mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 37mechanistic behaviorsupports2012Source 1needs review

LOV-PvuII variants displayed bidirectional polarity in photoactivation depending on the fusion interface, with increased DNA cleavage activity occurring either in the dark state or in the blue-light photoexcited state.

Depending on the particular fusion interface, the LOV-PvuII variants obtained had a bidirectional polarity in photoactivation; i.e., increased DNA cleavage activity was observed either in the dark state, with a compact folded LOV domain, or in the blue light photoexcitation state, when the LOV domain is partially unfolded.
Claim 38reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 39reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 40reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 41reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 42reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 43reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 44reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 45reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 46reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.
Claim 47reversibilitysupports2012Source 1needs review

The light-dependent effect on LOV-PvuII fusion enzyme activity was fully reversible over multiple photocycles.

The effect is fully reversible over multiple photocycles.

Approval Evidence

1 source1 linked approval claimfirst-pass slug lov2-domain-from-avena-sativa-phototropin1
Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII

Source:

engineering resultsupports

Fusion of the Avena sativa phototropin1 LOV2 domain to PvuII generated a genetically encoded light-controllable endonuclease.

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.

Source:

Comparisons

Source-backed strengths

The reported LOV-PvuII fusion generated a genetically encoded light-controllable endonuclease and showed a 3-fold difference in DNA cleavage activity between blue-light illumination and dark conditions. A notable feature is bidirectional photoactivation polarity, as different fusion interfaces produced higher activity either in the dark state or in the blue-light photoexcited state.

Source:

Here, we have fused the light-sensitive LOV2 domain from Avena sativa phototropin1 to the restriction enzyme PvuII to generate a genetically encoded, light-controllable endonuclease.

Compared with A. sativa LOV2 domain

LOV2 domain from Avena sativa phototropin1 and A. sativa LOV2 domain address a similar problem space.

Shared frame: same top-level item type; shared mechanisms: light-dependent allosteric switching; same primary input modality: light

Compared with EL346

LOV2 domain from Avena sativa phototropin1 and EL346 address a similar problem space.

Shared frame: same top-level item type; shared mechanisms: light-dependent allosteric switching; same primary input modality: light

Compared with LOV2 blue light sensory domain

LOV2 domain from Avena sativa phototropin1 and LOV2 blue light sensory domain address a similar problem space.

Shared frame: same top-level item type; shared mechanisms: light-dependent allosteric switching; same primary input modality: light

Ranked Citations

  1. 1.
    StructuralSource 1Bioconjugate Chemistry2012Claim 9Claim 10Claim 10

    Extracted from this source document.