Plant Physiology Preview Published on November 26, 2003; 10.1104/pp.103.029751
Received July 3, 2003
Returned for revision August 5, 2003
Accepted September 13, 2003
Overexpression of a Mutant Basic Helix-Loop-Helix Protein HFR1, HFR1- N105, Activates a Branch Pathway of Light Signaling in Arabidopsis
Ki-Young Yang , Young-Mi Kim , Seunghee Lee , Pill-Soon Song , and Moon-Soo Soh *
Kumho Life and Environmental Science Laboratory, 1 Oryong-Dong, Buk-Gu, Gwangju 500-712, Republic of Korea
* Corresponding author; email: mssoh{at}kkpc.com.
The HFR1, a basic helix-loop-helix protein, is required for a subset of phytochrome A-mediated photoresponses in Arabidopsis. Here, we show that overexpression of the HFR1- N105 mutant, which lacks the N-terminal 105 amino acids, confers exaggerated photoresponses even in darkness. Physiological analysis implied that overexpression of HFR1- N105 activated constitutively a branch pathway of light signaling that mediates a subset of photomorphogenic responses, including germination, de-etiolation, gravitropic hypocotyl growth, blocking of greening, and expression of some light-regulated genes such as CAB, DRT112, PSAE, PSBL, PORA, and XTR7, without affecting the light-responsiveness of anthocyanin accumulation and expression of other light-regulated genes such as CHS and PSBS. Although the end-of-day far-red light response and petiole elongation were suppressed in the HFR1- N105-overexpressing plants, flowering time was not affected by HFR1- N105. In addition, the HFR1- N105-overexpressing plants showed hypersensitive photoresponses in the inhibition of hypocotyl elongation, dependently on phytochrome A, FHY1, and FHY3 under FR light or phyB under R light, respectively. Moreover, our double mutant analysis suggested that the hypersensitive photoresponse is due to functional cooperation between HFR1- N105 and other light-signaling components including HY5, a basic leucine zipper protein. Taken together, our results of gain-of-function approach with HFR1- N105 suggest the existence of a complex and important basic helix-loop-helix protein-mediated transcriptional network controlling a branch pathway of light signaling and provide a useful framework for further genetic dissection of light-signaling network in Arabidopsis.
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