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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Trends Plant Sci. 2010 Sep 20;16(1):19–28. doi: 10.1016/j.tplants.2010.08.003

Figure 1.

Figure 1

The PIF-subfamily of phy-interacting basic helix–loop–helix (bHLH) transcription factors. (a) PIF3 domain structure. Schematic of the PIF3 polypeptide showing the location of the consensus bHLH domain, which defines this class of transcription factors, as well as the binding sites for photoactivated phyB (APB) and phyA (APA). The bHLH domain is responsible for dimerization and DNA-binding of the protein. The Arabidopsis PIFs bind to the conserved G-box DNA-sequence motif shown. (b) Subfamily 15 of the Arabidopsis bHLH family showing the phylogeny, nomenclature, domain structures, phy-interaction activity and in vivo functional activity of the PIF proteins. Pfr-specific interaction with phyA and/or phyB is indicated as A and/or B, and lack of interaction as (−). The asterisk indicates evidence of PIF8 binding to phyB (Y. Oka and P.H. Quail, unpublished). Evidence of functional involvement in phy signaling in vivo is indicated as (+), and lack of such evidence as (−). ND = not determined. Modified from [5, 10].