Source 1primary paper2016Molecular BioSystems
Toolkit/LOV-intein fusion protein
LOV-intein fusion protein
Also known as: chimera, fusion protein
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The LOV-intein fusion protein is a light-responsive chimera in which DnaE split inteins flank the Avena sativa LOV2 photosensory domain. It enables blue-light upregulation of intein splicing to control post-translational formation of a functional protein, and this behavior was reported in bacterial and human cells.
Usefulness & Problems
Why this is useful
This tool provides optical control over protein formation at the post-translational level rather than through transcriptional regulation. The reported activity in both bacterial and human cells indicates utility for light-triggered activation of proteins across distinct cellular contexts.
Source:
with blue light in bacterial and human cells
Source:
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
Problem solved
It addresses the problem of controlling when a functional protein is assembled after expression has occurred. Specifically, it uses blue light to increase intein splicing, thereby gating formation of the active protein product.
Source:
with blue light in bacterial and human cells
Problem links
Need precise spatiotemporal control with light input
DerivedThe LOV-intein fusion protein is a light-responsive chimera composed of DnaE split inteins flanking the Avena sativa LOV2 domain. It enables blue-light upregulation of intein splicing, thereby controlling post-translational formation of a functional protein.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
light-regulated intein splicinglight-regulated intein splicingpost-translational control of protein formationpost-translational control of protein formationTechniques
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 componentswitch architecture: split
The reported construct consists of DnaE split inteins flanking the Avena sativa LOV2 domain. Activation is driven by blue light, and the literature reports use in bacterial and human cells, but the supplied evidence does not include construct architecture details beyond the fusion composition or any delivery/expression protocol specifics.
The supplied evidence does not provide quantitative performance metrics such as dynamic range, kinetics, background splicing, or reversibility. It also does not specify target proteins, illumination parameters, or the breadth of validation beyond the reported bacterial and human cell contexts.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
Approval Evidence
1 source3 linked approval claimsfirst-pass slug lov-intein-fusion-protein
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa. The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
Source:
application contextsupports
Blue-light-controlled intein splicing with the LOV-intein fusion protein was reported in bacterial and human cells.
with blue light in bacterial and human cells
Source:
compositionsupports
The reported LOV-intein fusion protein consists of DnaE split-inteins flanking the light-sensitive Avena sativa LOV2 domain.
we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa
Source:
functionsupports
The LOV-intein fusion protein enables controlled formation of a functional protein by blue-light upregulation of intein splicing.
The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light
Source:
Comparisons
Source-backed strengths
The design directly couples a defined photosensory domain, Avena sativa LOV2, to DnaE split inteins in a single chimera. Reported function includes blue-light-induced upregulation of splicing and demonstration in both bacterial and human cells.
Compared with ArrayG
LOV-intein fusion protein 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
LOV-intein fusion protein 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
LOV-intein fusion protein 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.