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Arabidopsis Transcription Factor ELONGATED HYPOCOTYL5 Plays a Role in the Feedback Regulation of Phytochrome A Signaling
Author(s) -
Jigang Li,
Gang Li,
Shumin Gao,
Cristina Martínez,
Guangming He,
Zhenzhen Zhou,
Xi Huang,
JaeHoon Lee,
Huiyong Zhang,
Yunping Shen,
Haiyang Wang,
Xing Wang Deng
Publication year - 2010
Publication title -
the plant cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.324
H-Index - 341
eISSN - 1532-298X
pISSN - 1040-4651
DOI - 10.1105/tpc.110.075788
Subject(s) - photomorphogenesis , transcription factor , phytochrome a , biology , phytochrome , arabidopsis , microbiology and biotechnology , far red , transcription (linguistics) , promoter , signal transduction , dna binding protein , genetics , gene expression , botany , gene , red light , mutant , linguistics , philosophy
Phytochrome A (phyA) is the primary photoreceptor responsible for perceiving and mediating various responses to far-red light in Arabidopsis thaliana. FAR-RED ELONGATED HYPOCOTYL1 (FHY1) and its homolog FHY1-LIKE (FHL) are two small plant-specific proteins essential for light-regulated phyA nuclear accumulation and subsequent phyA signaling processes. FHY3 and its homolog FAR-RED IMPAIRED RESPONSE1 (FAR1) are two transposase-derived transcription factors that directly activate FHY1/FHL transcription and thus mediate subsequent phyA nuclear accumulation and responses. Here, we report that ELONGATED HYPOCOTYL5 (HY5), a well-characterized bZIP transcription factor involved in promoting photomorphogenesis, directly binds ACGT-containing elements a few base pairs away from the FHY3/FAR1 binding sites in the FHY1/FHL promoters. We demonstrate that HY5 physically interacts with FHY3/FAR1 through their respective DNA binding domains and negatively regulates FHY3/FAR1-activated FHY1/FHL expression under far-red light. Together, our data show that HY5 plays a role in negative feedback regulation of phyA signaling by attenuating FHY3/FAR1-activated FHY1/FHL expression, providing a mechanism for fine-tuning phyA signaling homeostasis.

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