Source 1primary paper2017The Plant Journal
Toolkit/CRY2-BIC1
CRY2-BIC1
Also known as: BIC1, blue-light inhibitor of cryptochromes 1, Blue-light Inhibitor of Cryptochromes 1
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
CRY2-BIC1 is a multi-component blue-light-dependent interacting protein pair derived from Arabidopsis thaliana cryptochrome 2 (CRY2) and Blue-light Inhibitor of Cryptochromes 1 (BIC1). It functions as a light-input protein interaction switch, and phage-assisted continuous evolution was applied to increase the dynamic range of the blue-light-dependent CRY2-BIC1 interaction.
Usefulness & Problems
Why this is useful
This tool provides optical control over protein association using blue light, enabling a genetically encoded input modality for regulating downstream biological processes. The available evidence specifically supports its development as a light-input switch and subsequent engineering to improve interaction dynamic range.
Source:
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
Problem solved
CRY2-BIC1 addresses the need for a blue-light-responsive protein interaction module that can be engineered for improved switching performance. The cited engineering work specifically targeted increasing the dynamic range of the light-dependent interaction.
Source:
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
Directed EvolutionTarget processes
recombinationInput: Light
Implementation Constraints
The tool is based on Arabidopsis thaliana CRY2 and BIC1, so implementation requires expression of at least these two components. The evidence also notes mutational analysis of 51 universally conserved CRY2 residues and identifies residues affecting stable expression of Arabidopsis CRY2 in plants, but it does not provide construct architecture or deployment details for the switch itself.
The supplied evidence does not report quantitative performance metrics, kinetic parameters, wavelength dependence beyond blue light, or validation across multiple cellular contexts. Independent replication of the engineered switch performance is not established from the provided sources.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2019eScholarship (California Digital Library)
Source 3primary paper2016Science
Ranked Claims
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
CRY and BIC form a negative-feedback circuitry that regulates each other's activity.
These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
CRY and BIC form a negative-feedback circuitry that regulates each other's activity.
These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
CRY and BIC form a negative-feedback circuitry that regulates each other's activity.
These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
CRY and BIC form a negative-feedback circuitry that regulates each other's activity.
These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
CRY and BIC form a negative-feedback circuitry that regulates each other's activity.
These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
CRY and BIC form a negative-feedback circuitry that regulates each other's activity.
These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
CRY and BIC form a negative-feedback circuitry that regulates each other's activity.
These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.
by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters
Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.
by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters
Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.
by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters
Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.
by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters
Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.
by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters
Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.
by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters
Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.
by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters
Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.
suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.
Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.
suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.
Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.
suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.
Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.
suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.
Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.
suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.
Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.
suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.
Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.
suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.
BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.
two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization
BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.
two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization
BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.
two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization
BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.
two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization
BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.
two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization
BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.
two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization
BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.
two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization
Cryptochromes mediate light activation of transcription of the BIC genes.
Here we show that cryptochromes mediate light activation of transcription of the BIC genes
Cryptochromes mediate light activation of transcription of the BIC genes.
Here we show that cryptochromes mediate light activation of transcription of the BIC genes
Cryptochromes mediate light activation of transcription of the BIC genes.
Here we show that cryptochromes mediate light activation of transcription of the BIC genes
Cryptochromes mediate light activation of transcription of the BIC genes.
Here we show that cryptochromes mediate light activation of transcription of the BIC genes
Cryptochromes mediate light activation of transcription of the BIC genes.
Here we show that cryptochromes mediate light activation of transcription of the BIC genes
Cryptochromes mediate light activation of transcription of the BIC genes.
Here we show that cryptochromes mediate light activation of transcription of the BIC genes
Cryptochromes mediate light activation of transcription of the BIC genes.
Here we show that cryptochromes mediate light activation of transcription of the BIC genes
Phytochromes also mediate light activation of BIC transcription.
Surprisingly, phytochromes also mediate light activation of BIC transcription
Phytochromes also mediate light activation of BIC transcription.
Surprisingly, phytochromes also mediate light activation of BIC transcription
Phytochromes also mediate light activation of BIC transcription.
Surprisingly, phytochromes also mediate light activation of BIC transcription
Phytochromes also mediate light activation of BIC transcription.
Surprisingly, phytochromes also mediate light activation of BIC transcription
Phytochromes also mediate light activation of BIC transcription.
Surprisingly, phytochromes also mediate light activation of BIC transcription
Phytochromes also mediate light activation of BIC transcription.
Surprisingly, phytochromes also mediate light activation of BIC transcription
Arabidopsis cryptochrome 2 undergoes blue light-dependent homodimerization to become physiologically active.
We found that Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active.
The authors hypothesize that regulated dimerization governs homeostasis of active cryptochromes in plants and other evolutionary lineages.
We hypothesize that regulated dimerization governs homeostasis of the active cryptochromes in plants and other evolutionary lineages.
BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
Approval Evidence
3 sources13 linked approval claimsfirst-pass slugs bic1, blue-light-inhibitor-of-cryptochromes-1, cry2-bic1
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1 (Blue-light Inhibitor of Cryptochromes 1)
Source:
Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2)
Source:
BIC1 (blue-light inhibitor of cryptochromes 1)
Source:
comparative expression stabilitysupports
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Source:
engineering outcomesupports
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
Source:
experimental resultsupports
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
Source:
mutational function retentionsupports
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
Source:
tool developmentsupports
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
Source:
variant isolationsupports
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
Source:
feedback circuitsupports
CRY and BIC form a negative-feedback circuitry that regulates each other's activity.
These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
Source:
pathway mechanismsupports
Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.
by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters
Source:
physiological functionsupports
Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.
suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.
Source:
regulatory mechanismsupports
BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.
two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization
Source:
transcriptional regulationsupports
Cryptochromes mediate light activation of transcription of the BIC genes.
Here we show that cryptochromes mediate light activation of transcription of the BIC genes
Source:
transcriptional regulationsupports
Phytochromes also mediate light activation of BIC transcription.
Surprisingly, phytochromes also mediate light activation of BIC transcription
Source:
inhibitory interactionsupports
BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
Source:
Comparisons
Source-backed strengths
The pair is explicitly described as a novel blue-light-dependent interacting protein system based on CRY2 and BIC1. Its performance was further optimized by phage-assisted continuous evolution, with evidence stating that dynamic range of the CRY2-BIC1 interaction was increased.
Source:
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Source:
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
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