ABSTRACT
Phytochrome A (phyA) is a red and far-red (FR) sensing photoreceptor regulating plant growth and development. Its biologically active FR-absorbing form Pfr translocates into the nucleus and subsequently regulates gene expression. Two transport facilitators, FR elongated hypocotyl 1 (FHY1) and FHY1-like (FHL), are crucial for its cytoplasmic-nuclear translocation. FHY1 interacts preferentially with activated phyA (Pfr) in assays with recombinant phyA and FHY1 and in vivo. Nuclear translocation of the phyA-FHY1 complex depends on a nuclear localization signal (NLS) of FHY1, which is recognized by IMPαs independently of phyA. The complex is guided along the actin cytoskeleton. Additionally, FHY1 has the ability to exit the nucleus via the exportin route, thus is able to repeatedly transport phyA molecules to the nucleus, balancing the nucleo-cytoplasmic distribution. The direction of FHY1s transport appears to depend on its phosphorylation state in different compartments. Phosphorylated serins close to the NLS prevent FHY1 binding to IMPα. The work presented here elucidates key steps of the mechanism by which photoactivated phyA translocates to the nucleus.
