Source 1primary paper1998The Plant Cell
Toolkit/CRY1
CRY1
Also known as: cry1, cryptochrome 1, Drosophila-like cry1 gene family
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
CRY1 is a blue-light-sensing cryptochrome protein from the Arabidopsis cryptochrome family, and the name cry1 is also used for a Drosophila-like insect cryptochrome gene family. The supplied evidence indicates that CRY1 mediates blue light responses, contributes to regulation of early blue light-induced genes, and has functional overlap with CRY2.
Usefulness & Problems
Why this is useful
CRY1 is useful as a genetically encoded blue-light-responsive protein domain for studying and engineering light-regulated developmental and transcriptional processes. The evidence also supports use of CRY1-derived domains in fusion constructs, because CRY1 and CRY2 domains were reported to be functionally interchangeable in transgenic plant overexpression experiments.
Source:
Previous studies have shown that insect CRY1 is photosensitive, whereas photo-insensitive CRY2 functions to potently inhibit clock-relevant CLOCK:CYCLE-mediated transcription.
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Comparison of the responses of the quadruple mutant cry1 cry2 phot1 phot2 to blue light with those of related triple mutants revealed that cryptochromes function in blue light-dependent, random hypocotyl-bending
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The two members of the Arabidopsis cryptochrome gene family (CRY1 and CRY2) overlap in function
Problem solved
CRY1 helps address the problem of controlling or dissecting blue light-dependent signaling and gene regulation in living systems. In the cited Arabidopsis studies, it was used to define receptor contributions to hypocotyl bending and early blue light-induced transcription, and in chimeric constructs to probe functional overlap and stability differences relative to CRY2.
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
degradationtranscriptionInput: Light
Implementation Constraints
The evidence supports implementation through domain fusion and transgenic overexpression in plants, including chimeric CRY1/CRY2 proteins. Blue light is the activating input, but the supplied literature excerpts do not specify wavelength ranges, cofactors, expression levels, or construct boundaries.
The supplied evidence does not define a specific engineered CRY1 optogenetic construct, quantitative photophysical parameters, or a minimal transferable domain with validated performance outside the cited plant transgenic context. The name CRY1 also spans Arabidopsis and insect family usage, so organismal context is important when interpreting function.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2007Molecular Biology and Evolution
Source 3primary paper2004Proceedings of the National Academy of Sciences
Ranked Claims
At least two rounds of gene duplication at the base of the metazoan radiation, together with several losses, gave rise to two cryptochrome gene families in insects: a Drosophila-like cry1 family and a vertebrate-like cry2 family.
Phylogenetic analyses show at least 2 rounds of gene duplication at the base of the metazoan radiation, as well as several losses, gave rise to 2 cryptochrome (cry) gene families in insects, a Drosophila-like cry1 gene family and a vertebrate-like cry2 family.
Previous studies showed that insect CRY1 is photosensitive, whereas photo-insensitive CRY2 potently inhibits CLOCK:CYCLE-mediated transcription.
Previous studies have shown that insect CRY1 is photosensitive, whereas photo-insensitive CRY2 functions to potently inhibit clock-relevant CLOCK:CYCLE-mediated transcription.
Cryptochromes function in blue light-dependent random hypocotyl-bending.
Comparison of the responses of the quadruple mutant cry1 cry2 phot1 phot2 to blue light with those of related triple mutants revealed that cryptochromes function in blue light-dependent, random hypocotyl-bending
cry1 and cry2 independently function as key regulators of early blue light-induced genes.
Microarray analysis suggested that cry1 and cry2 independently function as key regulators of early blue light-induced genes
CRY2 is rapidly degraded under activating light fluences whereas CRY1 is not.
cry2 is rapidly degraded under light fluences (green, blue, and UV) that activate the photoreceptor, but cry1 is not
Domains of CRY1 and CRY2 are functionally interchangeable in fusion constructs overexpressed in transgenic plants.
we demonstrate by overexpression in transgenic plants of cry1 and cry2 fusion constructs that their domains are functionally interchangeable
CRY1 and CRY2 overlap in function in Arabidopsis.
The two members of the Arabidopsis cryptochrome gene family (CRY1 and CRY2) overlap in function
Approval Evidence
4 sources12 linked approval claimsfirst-pass slug cry1
Blue light is sensed by the Arabidopsis photoreceptors CRY1 and CRY2
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a Drosophila-like cry1 gene family
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the cryptochromes cry1 and cry2
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The two members of the Arabidopsis cryptochrome gene family (CRY1 and CRY2) overlap in function
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comparative mechanismsupports
CRY1 and CRY2 differ strongly in their blue-light-induced interaction with the COP1/SPA complex.
In total, our results demonstrate that CRY1 and CRY2 strongly differ in their blue light-induced interaction with the COP1/SPA complex.
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dependencysupports
SPA proteins are required for the high-affinity blue-light-induced interaction between CRY1 and COP1 in vivo.
In a spa quadruple mutant that is devoid of all four SPA proteins, CRY1 and COP1 did not interact in vivo, neither in dark-grown nor in blue light-grown seedlings. Hence, SPA proteins are required for the high-affinity interaction between CRY1 and COP1 in blue light.
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domain requirementsupports
The coiled-coil domain of SPA1 is necessary to mediate a CRY1-SPA1 interaction in vivo.
The coiled-coil domain of SPA1 which is responsible for COP1-binding was necessary to mediate a CRY1-SPA1 interaction in vivo
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interaction enhancementsupports
SPA1 enhances the CRY1-COP1 interaction in yeast three-hybrid experiments.
Yeast three-hybrid experiments also show that SPA1 enhances the CRY1-COP1 interaction.
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light dependent interactionsupports
CRY1 and CRY2 form a complex with COP1 only after blue-light exposure and not in dark-grown seedlings.
our in vivo co-immunoprecipitation experiments suggest that CRY1 and CRY2 form a complex with COP1 only after seedlings were exposed to blue light. No association between COP1 and CRY1 or CRY2 was observed in dark-grown seedlings.
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evolutionary historysupports
At least two rounds of gene duplication at the base of the metazoan radiation, together with several losses, gave rise to two cryptochrome gene families in insects: a Drosophila-like cry1 family and a vertebrate-like cry2 family.
Phylogenetic analyses show at least 2 rounds of gene duplication at the base of the metazoan radiation, as well as several losses, gave rise to 2 cryptochrome (cry) gene families in insects, a Drosophila-like cry1 gene family and a vertebrate-like cry2 family.
Source:
functional propertysupports
Previous studies showed that insect CRY1 is photosensitive, whereas photo-insensitive CRY2 potently inhibits CLOCK:CYCLE-mediated transcription.
Previous studies have shown that insect CRY1 is photosensitive, whereas photo-insensitive CRY2 functions to potently inhibit clock-relevant CLOCK:CYCLE-mediated transcription.
Source:
functional rolesupports
Cryptochromes function in blue light-dependent random hypocotyl-bending.
Comparison of the responses of the quadruple mutant cry1 cry2 phot1 phot2 to blue light with those of related triple mutants revealed that cryptochromes function in blue light-dependent, random hypocotyl-bending
Source:
transcriptional regulation rolesupports
cry1 and cry2 independently function as key regulators of early blue light-induced genes.
Microarray analysis suggested that cry1 and cry2 independently function as key regulators of early blue light-induced genes
Source:
differential stabilitysupports
CRY2 is rapidly degraded under activating light fluences whereas CRY1 is not.
cry2 is rapidly degraded under light fluences (green, blue, and UV) that activate the photoreceptor, but cry1 is not
Source:
domain interchangeabilitysupports
Domains of CRY1 and CRY2 are functionally interchangeable in fusion constructs overexpressed in transgenic plants.
we demonstrate by overexpression in transgenic plants of cry1 and cry2 fusion constructs that their domains are functionally interchangeable
Source:
functional overlapsupports
CRY1 and CRY2 overlap in function in Arabidopsis.
The two members of the Arabidopsis cryptochrome gene family (CRY1 and CRY2) overlap in function
Source:
Comparisons
Source-backed strengths
The evidence supports that CRY1 is intrinsically photosensitive and senses blue light. In Arabidopsis, CRY1 independently regulates early blue light-induced genes, participates in blue light-dependent random hypocotyl-bending, overlaps functionally with CRY2, and is more stable than CRY2 under activating light fluences because CRY2 is rapidly degraded whereas CRY1 is not.
Ranked Citations
- 1.
- 2.
Derived from 2 linked claims. Example evidence: Phylogenetic analyses show at least 2 rounds of gene duplication at the base of the metazoan radiation, as well as several losses, gave rise to 2 cryptochrome (cry) gene families in insects, a Drosophila-like cry1 gene family and a vertebrate-like cry2 family.
- 3.
Derived from 2 linked claims. Example evidence: Comparison of the responses of the quadruple mutant cry1 cry2 phot1 phot2 to blue light with those of related triple mutants revealed that cryptochromes function in blue light-dependent, random hypocotyl-bending