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Phytochrome C And Low Temperature Promote The Expression And Red Light Signaling Of Phytochrome D

ABSTRACT: Phytochrome C And Low Temperature Promote The Expression And Red Light Signaling Of Phytochrome D

PROVIDER: PRJNA1063695 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27500300_1.fastq.gz	Fastqsanger.gz
	SRR27500300_2.fastq.gz	Fastqsanger.gz
	SRR27500301_1.fastq.gz	Fastqsanger.gz
	SRR27500301_2.fastq.gz	Fastqsanger.gz
	SRR27500302_1.fastq.gz	Fastqsanger.gz

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Phytochrome C and Low Temperature Promote the Expression and Red Light Signaling of Phytochrome D

Project description:Phytochrome C and Low Temperature Promote the Expression and Red Light Signaling of Phytochrome D

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Phytochrome C And Low Temperature Promote The Expression And Red Light Signaling Of Phytochrome D

Project description:Light is an ever-changing environmental parameter affecting almost every aspects of plant growth and development. It is perceived by photoreceptors, among them phytochromes (PHY) are responsible for monitoring the red and far-red part of the spectrum. Arabidopsis thaliana possesses five phytochromes genes, named through phyA-phyE. Whereas the function of phyA and phyB – that mediate most of the phytochrome responses – is extensively studied, our knowledge on other phytochromes are still rudimentary. To analyze phyD function we expressed it at high levels in different phytochrome deficient genetic backgrounds. We found that overexpressed phyD governs effective light signaling at low temperatures but only in cooperation with functional phyC. Under these conditions, opposite to phyB, phyD accumulates to high levels and this pool is stable under light illumination. Furthermore, the detectable photoconvertible phyD amount is proportional with the available protein amount indicating that the phyD pool contains fully functional photoreceptors. The thermal reversion of phyD is very fast suggesting that the thermosensing of phyD is based on its protein amount and not on its Pfr conformer stability, which was described for phyB. We also found that phyD and phyB associate to identical genomic locations and mediate similar gene expression changes, however the efficiency of phyD is lower. Taken together our data suggest that under certain conditions synergistic interaction of phyD and phyC substitutes phyB function thus increases the ability of plants to respond more flexible to environmental changes.

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Phytochrome C and Low Temperature Promote the Expression and Red Light Signaling of Phytochrome D

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mRNA-seq of Physcomitrella protonema responding to 1 hr red light in wild type and the phytochrome-deficient mutant

Project description:The red/far-red light photoreceptor phytochrome mediates photomorphological responses in plants. For light sensing and signaling, phytochromes need to associate with open-chain tetrapyrrole molecules as the chromophore. Biosynthesis of tetrapyrrole chromophores requires members of ferredoxin-dependent bilin reductases (FDBRs). There are two FDBRs in Physcomitrella patens, HY2 and PUBS. Knocking out both generates the phytochrome-deficient mutant. Datasets here provides the transcriptome profiling of Physcomitrella protonema grown in the dark and exposed to one hour red light. Wild type and the hy2 pubs double mutant were used to dissect the regulated genes of moss phytochromes. For details, please see PMID: .

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Phytochrome Interacting Factors 4 and 5 redundantly limit seedling de-etiolation in continuous far-red light.

Project description:Phytochromes are red/far red photosensors regulating numerous developmental programs in plants. Among them phytochrome A (phyA) is essential to enable seedling de-etiolation in continuous far-red (FR) light a condition mimicking the environment under a dense canopy. The ecological relevance of this response is demonstrated by the high mortality rate of phyA mutants germinating in deep vegetational shade. phyA signaling involves a direct interaction of the photoreceptor with members of the bHLH transcription factor family, PIF1 and PIF3 (Phytochrome Interacting Factor). Here we investigated the involvement of PIF4 and PIF5 in phyA signaling and found that they redundantly control de-etiolation in FR light. The pif4pif5 double mutant is hypersensitive to low fluence rates of FR light. This phenotype is dependent on FR light perception by phyA but does not rely on alterations of the phyA level. Our microarrays analysis shows that PIF4 and PIF5 are part of an inhibitory mechanism repressing the expression of some light-responsive genes in the dark and are also needed for full expression of several growth-related genes in the light. Unlike PIF1 and PIF3, PIF4 and PIF5 are not degraded in response to FR light indicating that they are light-regulated by a different mechanism. Our genetic analysis suggests that this is achieved through the sequestration of these PIFs by the closely related bHLH transcription factor HFR1 (long Hypocotyl in FR light).

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