Toolkit/HY5
HY5
Also known as: Arabidopsis bZIP protein HY5, Arabidopsis bZIP Protein HY5, Arabidopsis HY5, ELONGATED HYPOCOTYL 5, HY5
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
HY5 is an Arabidopsis thaliana basic leucine zipper (bZIP) transcription factor that directly binds light-responsive promoters and functions as a positive regulator of photomorphogenesis. It also mediates crosstalk between light signaling and the unfolded protein response (UPR) by negatively regulating UPR gene expression through promoter competition.
Usefulness & Problems
Why this is useful
HY5 is useful as a native plant transcriptional regulator for studying and potentially engineering light-regulated transcriptional programs in Arabidopsis. The cited evidence also supports its use for probing how light signaling interfaces with ER stress and UPR transcriptional control.
Problem solved
HY5 helps address the problem of linking external light cues to specific promoter occupancy and transcriptional outputs in plants. It also provides a defined molecular node for dissecting how light signaling antagonizes UPR gene activation through competition at a G-box-like cis-element in ERSE.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
competitive promoter bindingdna bindingDNA Bindinglight-signaling pathway crosstalktranscriptional regulationTechniques
No technique tags yet.
Target processes
transcriptionInput: Light
Implementation Constraints
The evidence supports HY5 as an Arabidopsis bZIP transcription factor acting through direct promoter interaction, including competition with bZIP28 at a G-box-like element within ERSE. No practical details are provided here on construct architecture, expression systems, cofactors, delivery methods, or minimal functional domains for engineered use.
The supplied evidence is confined to Arabidopsis and does not provide quantitative binding affinities, kinetic properties, or domain-level engineering parameters for tool deployment. It also does not establish HY5 as an exogenous modular part or validate performance across heterologous systems, cell types, or non-plant organisms.
Validation
Supporting Sources
Ranked Claims
Enhanced ER stress tolerance of hy5 plants is attributed to higher expression of UPR genes.
This enhanced tolerance of hy5 plants can be attributed to higher expression of UPR genes
Enhanced ER stress tolerance of hy5 plants is attributed to higher expression of UPR genes.
This enhanced tolerance of hy5 plants can be attributed to higher expression of UPR genes
Enhanced ER stress tolerance of hy5 plants is attributed to higher expression of UPR genes.
This enhanced tolerance of hy5 plants can be attributed to higher expression of UPR genes
Enhanced ER stress tolerance of hy5 plants is attributed to higher expression of UPR genes.
This enhanced tolerance of hy5 plants can be attributed to higher expression of UPR genes
Enhanced ER stress tolerance of hy5 plants is attributed to higher expression of UPR genes.
This enhanced tolerance of hy5 plants can be attributed to higher expression of UPR genes
Enhanced ER stress tolerance of hy5 plants is attributed to higher expression of UPR genes.
This enhanced tolerance of hy5 plants can be attributed to higher expression of UPR genes
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.
HY5 negatively regulates the unfolded protein response by competing with bZIP28 for binding to a G-box-like element in ERSE.
HY5 negatively regulates the UPR by competing with basic leucine zipper 28 (bZIP28) to bind to the G-box-like element present in the ER stress response element (ERSE)
HY5 negatively regulates the unfolded protein response by competing with bZIP28 for binding to a G-box-like element in ERSE.
HY5 negatively regulates the UPR by competing with basic leucine zipper 28 (bZIP28) to bind to the G-box-like element present in the ER stress response element (ERSE)
HY5 negatively regulates the unfolded protein response by competing with bZIP28 for binding to a G-box-like element in ERSE.
HY5 negatively regulates the UPR by competing with basic leucine zipper 28 (bZIP28) to bind to the G-box-like element present in the ER stress response element (ERSE)
HY5 negatively regulates the unfolded protein response by competing with bZIP28 for binding to a G-box-like element in ERSE.
HY5 negatively regulates the UPR by competing with basic leucine zipper 28 (bZIP28) to bind to the G-box-like element present in the ER stress response element (ERSE)
HY5 negatively regulates the unfolded protein response by competing with bZIP28 for binding to a G-box-like element in ERSE.
HY5 negatively regulates the UPR by competing with basic leucine zipper 28 (bZIP28) to bind to the G-box-like element present in the ER stress response element (ERSE)
HY5 negatively regulates the unfolded protein response by competing with bZIP28 for binding to a G-box-like element in ERSE.
HY5 negatively regulates the UPR by competing with basic leucine zipper 28 (bZIP28) to bind to the G-box-like element present in the ER stress response element (ERSE)
HY5 mediates crosstalk between light signaling and the unfolded protein response, acting positively in light signaling and negatively on UPR gene expression.
we propose a molecular mechanism of crosstalk between the UPR and light signaling, mediated by HY5, which positively mediates light signaling, but negatively regulates UPR gene expression
HY5 mediates crosstalk between light signaling and the unfolded protein response, acting positively in light signaling and negatively on UPR gene expression.
we propose a molecular mechanism of crosstalk between the UPR and light signaling, mediated by HY5, which positively mediates light signaling, but negatively regulates UPR gene expression
HY5 mediates crosstalk between light signaling and the unfolded protein response, acting positively in light signaling and negatively on UPR gene expression.
we propose a molecular mechanism of crosstalk between the UPR and light signaling, mediated by HY5, which positively mediates light signaling, but negatively regulates UPR gene expression
HY5 mediates crosstalk between light signaling and the unfolded protein response, acting positively in light signaling and negatively on UPR gene expression.
we propose a molecular mechanism of crosstalk between the UPR and light signaling, mediated by HY5, which positively mediates light signaling, but negatively regulates UPR gene expression
HY5 mediates crosstalk between light signaling and the unfolded protein response, acting positively in light signaling and negatively on UPR gene expression.
we propose a molecular mechanism of crosstalk between the UPR and light signaling, mediated by HY5, which positively mediates light signaling, but negatively regulates UPR gene expression
HY5 mediates crosstalk between light signaling and the unfolded protein response, acting positively in light signaling and negatively on UPR gene expression.
we propose a molecular mechanism of crosstalk between the UPR and light signaling, mediated by HY5, which positively mediates light signaling, but negatively regulates UPR gene expression
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
Mutation of HY5 leads to tolerance to ER stress.
mutation of the ELONGATED HYPOCOTYL 5 (HY5), a key component of light signaling, leads to tolerance to ER stress
Mutation of HY5 leads to tolerance to ER stress.
mutation of the ELONGATED HYPOCOTYL 5 (HY5), a key component of light signaling, leads to tolerance to ER stress
Mutation of HY5 leads to tolerance to ER stress.
mutation of the ELONGATED HYPOCOTYL 5 (HY5), a key component of light signaling, leads to tolerance to ER stress
Mutation of HY5 leads to tolerance to ER stress.
mutation of the ELONGATED HYPOCOTYL 5 (HY5), a key component of light signaling, leads to tolerance to ER stress
Mutation of HY5 leads to tolerance to ER stress.
mutation of the ELONGATED HYPOCOTYL 5 (HY5), a key component of light signaling, leads to tolerance to ER stress
Mutation of HY5 leads to tolerance to ER stress.
mutation of the ELONGATED HYPOCOTYL 5 (HY5), a key component of light signaling, leads to tolerance to ER stress
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.
HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions.
we found that HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions
HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions.
we found that HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions
HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions.
we found that HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions
HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions.
we found that HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions
HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions.
we found that HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions
HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions.
we found that HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions
Increasing light intensity elevates ER stress sensitivity in plants.
we demonstrate that increasing light intensity elevates the ER stress sensitivity of plants
Increasing light intensity elevates ER stress sensitivity in plants.
we demonstrate that increasing light intensity elevates the ER stress sensitivity of plants
Increasing light intensity elevates ER stress sensitivity in plants.
we demonstrate that increasing light intensity elevates the ER stress sensitivity of plants
Increasing light intensity elevates ER stress sensitivity in plants.
we demonstrate that increasing light intensity elevates the ER stress sensitivity of plants
Increasing light intensity elevates ER stress sensitivity in plants.
we demonstrate that increasing light intensity elevates the ER stress sensitivity of plants
Increasing light intensity elevates ER stress sensitivity in plants.
we demonstrate that increasing light intensity elevates the ER stress sensitivity of plants
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
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
HY5 directly interacts with light-responsive promoters.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 directly interacts with light-responsive promoters.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 directly interacts with light-responsive promoters.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 directly interacts with light-responsive promoters.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 directly interacts with light-responsive promoters.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 directly interacts with light-responsive promoters.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 directly interacts with light-responsive promoters.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
HY5 mediates light control of gene expression.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 mediates light control of gene expression.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 mediates light control of gene expression.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 mediates light control of gene expression.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 mediates light control of gene expression.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 mediates light control of gene expression.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 mediates light control of gene expression.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
Approval Evidence
ELONGATED HYPOCOTYL 5 (HY5)
Source:
mutation of the ELONGATED HYPOCOTYL 5 (HY5), a key component of light signaling
Source:
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
Source:
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
Source:
Enhanced ER stress tolerance of hy5 plants is attributed to higher expression of UPR genes.
This enhanced tolerance of hy5 plants can be attributed to higher expression of UPR genes
Source:
HY5 negatively regulates the unfolded protein response by competing with bZIP28 for binding to a G-box-like element in ERSE.
HY5 negatively regulates the UPR by competing with basic leucine zipper 28 (bZIP28) to bind to the G-box-like element present in the ER stress response element (ERSE)
Source:
HY5 mediates crosstalk between light signaling and the unfolded protein response, acting positively in light signaling and negatively on UPR gene expression.
we propose a molecular mechanism of crosstalk between the UPR and light signaling, mediated by HY5, which positively mediates light signaling, but negatively regulates UPR gene expression
Source:
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:
Mutation of HY5 leads to tolerance to ER stress.
mutation of the ELONGATED HYPOCOTYL 5 (HY5), a key component of light signaling, leads to tolerance to ER stress
Source:
HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions.
we found that HY5 undergoes 26S proteasome-mediated degradation under ER stress conditions
Source:
Increasing light intensity elevates ER stress sensitivity in plants.
we demonstrate that increasing light intensity elevates the ER stress sensitivity of plants
Source:
HY5 binds specifically to G-box DNA sequences and not to other examined light-responsive elements.
In vitro DNA binding studies suggested that HY5 can bind specifically to the G-box DNA sequences but not to any of the other LREs present in the light-responsive promoters examined.
Source:
Phytochrome-mediated red light- and far-red light-reversible low-fluence induction of G-box-containing promoters is diminished in hy5 plants.
the characteristic phytochrome-mediated red light- and far-red light-reversible low-fluence induction of the G-box-containing promoters was diminished specifically in hy5 plants
Source:
HY5 may directly interact with the G-box in promoters of light-inducible genes to mediate light-controlled transcriptional activity.
These results suggest that HY5 may interact directly with the G-box in the promoters of light-inducible genes to mediate light-controlled transcriptional activity.
Source:
HY5 is a basic leucine zipper transcription factor.
The Arabidopsis HY5 gene has been defined genetically as a positive regulator of photomorphogenesis and recently has been shown to encode a basic leucine zipper type of transcription factor.
Source:
HY5 directly interacts with light-responsive promoters.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
Source:
High-irradiance light activation of G-box-containing synthetic promoters and the RBCS-1A promoter is significantly compromised in the hy5 mutant.
High-irradiance light activation of two synthetic promoters containing either the consensus G-box alone or the G-box combined with the GATA motif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBCS-1A promoter, which has an essential copy of the G-box, was significantly compromised in the hy5 mutant.
Source:
HY5 is involved in light regulation of transcriptional activity of promoters containing the G-box.
HY5 is constitutively nuclear localized and is involved in light regulation of transcriptional activity of the promoters containing the G-box
Source:
HY5 mediates light control of gene expression.
Arabidopsis bZIP Protein HY5 Directly Interacts with Light-Responsive Promoters in Mediating Light Control of Gene Expression
Source:
HY5 is constitutively nuclear localized.
Here, we report that HY5 is constitutively nuclear localized
Source:
The effect of the hy5 mutation on high-irradiance light activation of gene expression occurs in both photosynthetic and nonphotosynthetic tissues.
The hy5 mutation's effect on the high-irradiance light activation of gene expression was observed in both photosynthetic and nonphotosynthetic tissues.
Source:
Comparisons
Source-backed strengths
The evidence identifies HY5 as a genetically defined positive regulator of photomorphogenesis and a bZIP transcription factor that directly interacts with light-responsive promoters. Additional mechanistic evidence shows that HY5 negatively regulates the UPR by competing with bZIP28 for binding to a G-box-like element in ERSE, and hy5 plants display enhanced ER stress tolerance associated with higher UPR gene expression.
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