The central coiled-coil domain and carboxyl-terminal WD-repeat domain of Arabidopsis SPA1 are responsible for mediating repression of light signaling.

Arabidopsis constitutive photomorphogenic 1 (COP1) is an E3 ubiquitin ligase that directly binds and targets for degradation a number of photomorphogenesis-promoting transcription factors, including HY5 and HFR1, to desensitize light signaling. Arabidopsis suppressor of phyA-105 (SPA1), which encodes a protein structurally related to COP1, also acts to repress photomorphogenesis under various light conditions. Here we show that overexpression of Arabidopsis SPA1 results in a hyperetiolation phenotype and reduced accumulation of HY5 and HFR1. In addition, we show that both COP1 and SPA1 are each dependent on the presence of the other for their repressive effect on light signaling. Moreover, we demonstrate that both the central coiled-coil and the C-terminal WD-repeat domains of SPA1 are necessary, and together these two domains are sufficient for repressing photomorphogenesis. However, the N-terminal kinase-like domain of SPA1 contributes to its full activity and promotes destabilization of the SPA1 protein. Together, our results substantiate the notion that COP1 and SPA1 act in concert to form a functional E3 ubiquitin ligase complex and provide a molecular basis for understanding the structure-function relationship of SPA1.