Plant Transcription Factor Database
Previous version: v3.0
Brassica oleracea
FAR1 Family
Species TF ID Description
XP_013583896.1FAR1 family protein
XP_013584280.1FAR1 family protein
XP_013585848.1FAR1 family protein
XP_013585849.1FAR1 family protein
XP_013586359.1FAR1 family protein
XP_013587988.1FAR1 family protein
XP_013588568.1FAR1 family protein
XP_013588569.1FAR1 family protein
XP_013588570.1FAR1 family protein
XP_013591899.1FAR1 family protein
XP_013592035.1FAR1 family protein
XP_013592036.1FAR1 family protein
XP_013592150.1FAR1 family protein
XP_013597789.1FAR1 family protein
XP_013597797.1FAR1 family protein
XP_013602010.1FAR1 family protein
XP_013602011.1FAR1 family protein
XP_013602012.1FAR1 family protein
XP_013602013.1FAR1 family protein
XP_013607599.1FAR1 family protein
XP_013607605.1FAR1 family protein
XP_013614667.1FAR1 family protein
XP_013615310.1FAR1 family protein
XP_013621323.1FAR1 family protein
XP_013621324.1FAR1 family protein
XP_013621325.1FAR1 family protein
XP_013621581.1FAR1 family protein
XP_013621583.1FAR1 family protein
XP_013621584.1FAR1 family protein
XP_013629186.1FAR1 family protein
XP_013629187.1FAR1 family protein
XP_013630078.1FAR1 family protein
XP_013630454.1FAR1 family protein
XP_013634181.1FAR1 family protein
XP_013634182.1FAR1 family protein
XP_013637168.1FAR1 family protein
XP_013637169.1FAR1 family protein
XP_013637170.1FAR1 family protein
XP_013637171.1FAR1 family protein
FAR1 Family Introduction

We show that Arabidopsis FHY3 and FAR1, which encode two proteins related to Mutator-like transposases, act together to modulate phyA signaling by directly activating the transcription of FHY1 and FHL, whose products are essential for light-induced phyA nuclear accumulation and subsequent light responses. FHY3 and FAR1 have separable DNA binding and transcriptional activation domains that are highly conserved in Mutator-like transposases. Further, expression of FHY3 and FAR1 is negatively regulated by phyA signaling. We propose that FHY3 and FAR1 represent transcription factors that have been co-opted from an ancient Mutator-like transposase(s) to modulate phyA-signaling homeostasis in higher plants.

We next used a yeast one-hybrid assay to delineate the DNA sequences to which FHY3 and FAR1 bind. GAD-FHY3 or GAD-FAR1 fusion proteins (GAD, GAL4 transcriptional activation domain), but not GAD alone, activated the LacZ reporter genes driven by the FHY1 and FHL promoters. Deletion analysis narrowed down the FHY3/FAR1 binding site to a 39-bp promoter subfragment located on the "a" fragment for both FHY1 and FHL. Notably, these subfragments share a stretch of consensus sequence, 5'-TTCACGCGCC-3'. Mutating the core sequence "CACGCGC" of this motif (m2 and m3 for FHY1, m5 for FHL) abolished the reporter gene activation by both GAD-FHY3 and GAD-FAR1. Mutating the flanking sequences (m1 and m4) did not obviously affect the reporter gene activation by GAD-FAR1, but clearly reduced activation by GAD-FHY3. Thus, "CACGCGC" likely defines a cis-element that confers specific binding for FHY3 and FAR1 and is named FBS for FHY3-FAR1 binding site.

Lin R, Ding L, Casola C, Ripoll DR, Feschotte C, Wang H.
Transposase-derived transcription factors regulate light signaling in Arabidopsis.
Science, 2007. 318(5854): p. 1302-5.
PMID: 18033885