Functional demonstration of Aureochrome 1a proteasomal degradation after blue light incubation in the diatom Phaeodactylum tricornutum.

Aureochromes (AUREOs) are both blue light photoreceptors and transcription factors found in diatoms and related algal groups that play a critical role in regulating gene and cell physiology. One of the AUREOs in the diatom Phaeodactylum tricornutum, PtAUREO1a, has been demonstrated to significantly influence global cellular transcription upon blue light exposure. PtAUREO1a itself is highly regulated on the gene transcription level, depending on the light conditions. However, little is known about the proteostasis of PtAUREO1a in vivo. In this study, we used quantitative immunoblot analysis to examine PtAUREO1a levels under different light conditions as well as in the presence of inhibitors for translation and proteolysis. Our results demonstrate that PtAUREO1a is rapidly degraded in response to blue light exposure after red light acclimation, while the protein has an extended protein half-life in white light conditions. Moreover, the data provide the first in vivo evidence for a functional ubiquitin-proteasome system in the model diatom P. tricornutum. Our findings provide a theoretical basis for studies on protein degradation mechanisms and the regulation of PtAUREO1a, suggesting that changing light conditions can have an impact on the PtAUREO1a protein amount by directly affecting its protein stability.