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Chaperone-like protein DAY plays critical roles in photomorphogenesis

ABSTRACT: Chaperone-like protein DAY plays critical roles in photomorphogenesis

PROVIDER: PRJNA736856 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14785520.fastq.gz	Fastqsanger.gz
	SRR14785521.fastq.gz	Fastqsanger.gz
	SRR14785522.fastq.gz	Fastqsanger.gz
	SRR14785523.fastq.gz	Fastqsanger.gz
	SRR14785524.fastq.gz	Fastqsanger.gz

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Chaperone-like protein DAY plays critical roles in photomorphogenesis.

Project description:Photomorphogenesis, light-mediated development, is an essential feature of all terrestrial plants. While chloroplast development and brassinosteroid (BR) signaling are known players in photomorphogenesis, proteins that regulate both pathways have yet to be identified. Here we report that DE-ETIOLATION IN THE DARK AND YELLOWING IN THE LIGHT (DAY), a membrane protein containing DnaJ-like domain, plays a dual-role in photomorphogenesis by stabilizing the BR receptor, BRI1, as well as a key enzyme in chlorophyll biosynthesis, POR. DAY localizes to both the endomembrane and chloroplasts via its first transmembrane domain and chloroplast transit peptide, respectively, and interacts with BRI1 and POR in their respective subcellular compartments. Using genetic analysis, we show that DAY acts independently on BR signaling and chlorophyll biogenesis. Collectively, this work uncovers DAY as a factor that simultaneously regulates BR signaling and chloroplast development, revealing a key regulator of photomorphogenesis that acts across cell compartments.

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Chaperone-like protein DAY plays critical roles in photomorphogenesis

Project description:We found that the transcriptome of day RNAi seedlings significantly overlaps with that of the bri1-116 mutant, especially in the dark. These data indicate that DAY acts as a positive regulator of BR signaling.

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