title: Blue light induces degradation of the negative regulator phytochrome interacting factor 1 to promote photomorphogenic development of Arabidopsis seedlings.
abstract: Phytochrome interacting factors (PIFs) are nuclear basic helix-loop-helix (bHLH) transcription factors that negatively regulate photomorphogenesis both in the dark and in the light in Arabidopsis. The phytochrome (phy) family of photoreceptors induces the rapid phosphorylation and degradation of PIFs in response to both red and far-red light conditions to promote photomorphogenesis. Although phys have been shown to function under blue light conditions, the roles of PIFs under blue light have not been investigated in detail. Here we show that PIF1 negatively regulates photomorphogenesis at the seedling stage under blue light conditions. pif1 seedlings displayed more open cotyledons and slightly reduced hypocotyl length compared to wild type under diurnal (12 hr light/12 hr dark) blue light conditions. Double-mutant analyses demonstrated that pif1phyA, pif1phyB, pif1cry1, and pif1cry2 have enhanced cotyledon opening compared to the single photoreceptor mutants under diurnal blue light conditions. Blue light induced the rapid phosphorylation, polyubiquitination, and degradation of PIF1 through the ubi/26S proteasomal pathway. PIF1 interacted with phyA and phyB in a blue light-dependent manner, and the interactions with phys are necessary for the blue light-induced degradation of PIF1. phyA played a dominant role under pulses of blue light, while phyA, phyB, and phyD induced the degradation of PIF1 in an additive manner under prolonged continuous blue light conditions. Interestingly, the absence of cry1 and cry2 enhanced the degradation of PIF1 under blue light conditions. Taken together, these data suggest that PIF1 functions as a negative regulator of photomorphogenesis under blue light conditions and that blue light-activated phys induce the degradation of PIF1 through the ubi/26S proteasomal pathway to promote photomorphogenesis.
authors.affiliation: University of Texas, Austin, Texas 78712, USA.
authors.forename: Alicia
authors.initials: A
authors.lastname: Castillon
authors.forename: Hui
authors.initials: H
authors.lastname: Shen
authors.forename: Enamul
authors.initials: E
authors.lastname: Huq
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism* / Q000528:radiation effects; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism*; D051792:Basic Helix-Loop-Helix Proteins / Q000235:genetics* / Q000378:metabolism*; D015153:Blotting, Western; D056931:Cryptochromes; D005420:Flavoproteins / Q000235:genetics / Q000378:metabolism; D047468:Immunoprecipitation; D008027:Light; D010766:Phosphorylation; D010786:Photoreceptor Cells / Q000528:radiation effects; D051942:Phytochrome A / Q000235:genetics / Q000378:metabolism; D051939:Phytochrome B / Q000235:genetics / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D036226:Seedlings / Q000166:cytology* / Q000502:physiology* / Q000528:radiation effects; D020798:Two-Hybrid System Techniques; D054875:Ubiquitination
chemical_list: D029681:Arabidopsis Proteins; D051792:Basic Helix-Loop-Helix Proteins; D056931:Cryptochromes; D005420:Flavoproteins; D051942:Phytochrome A; D051939:Phytochrome B; D046988:Proteasome Endopeptidase Complex; D012333:RNA, Messenger; C538962:CRY1 protein, Arabidopsis; C103618:CRY2 protein, Arabidopsis; C508068:At2g20180 protein, Arabidopsis; C061553:ATP dependent 26S protease