z-logo
open-access-imgOpen Access
FAR-RED ELONGATED HYPOCOTYL1 and FHY1-LIKE Associate with theArabidopsisTranscription Factors LAF1 and HFR1 to Transmit Phytochrome A Signals for Inhibition of Hypocotyl Elongation
Author(s) -
Seong Wook Yang,
InCheol Jang,
Rossana Henriques,
NamHai Chua
Publication year - 2009
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.109.067215
Subject(s) - phytochrome a , biology , transcription factor , arabidopsis , phytochrome , hypocotyl , mutant , microbiology and biotechnology , elongation factor , arabidopsis thaliana , far red , transcription (linguistics) , genetics , immunoprecipitation , gene , botany , rna , red light , ribosome , linguistics , philosophy
Among the five phytochromes in Arabidopsis thaliana, phytochrome A (phyA) plays a major role in seedling deetiolation. Mutant analyses have identified more than 10 positive components acting downstream of phyA to inhibit hypocotyl elongation. However, their sites of action and their hierarchical relationships are poorly understood. Here, we investigated the genetic and molecular relationship between two homologous proteins, FAR-RED ELONGATED HYPOCOTYL1 (FHY1) and FHY1-LIKE (FHL), and two transcription factors, LONG AFTER FAR-RED LIGHT1 (LAF1) and LONG HYPOCOTYL IN FAR-RED1 (HFR1). Analyses of double and triple mutants showed that LAF1, a myb factor, and HFR1, a basic helix-loop-helix factor, independently transmit phyA signals downstream of FHY1 and FHL. Coimmunoprecipitation experiments showed that phyA, FHY1, FHL, LAF1, and HFR1 are components of protein complexes in vivo. In vitro pull-down assays demonstrated direct interactions between partner proteins with the N-terminal region of FHY1, as well as that of FHL, interacting with the LAF1 N-terminal portion and the HFR1 C-terminal region. These results suggest that, in addition to assisting phyA nuclear accumulation, FHY1 and FHL are required to assemble photoreceptor/transcription factor complexes for phyA signaling.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom