14-3-3 Proteins Regulate Intracellular Localization of the bZIP Transcriptional Activator RSG

Abstract

Gibberellins (GAs) are essential regulators of many aspects of plant development, including stem elongation, seed germination, and flowering. RSG is a transcriptional activator with a basic leucine zipper domain that regulates endogenous amounts of GAs through the control of a GA biosynthetic enzyme. The ubiquitous expression of RSG in plant organs suggests an involvement of post-transcriptional and/or post-translational modifications of the transcription factor. Here, we identify the 14-3-3 signaling proteins as RSG binding partners. The mutant version of RSG that could not bind to 14-3-3 proteins exhibited a higher transcriptional activity than did wild-type RSG. Consistent with this observation, the mutant RSG that could not bind to 14-3-3 proteins was localized predominantly in the nucleus, whereas wild-type RSG was distributed throughout the cell. Using the nuclear export inhibitor leptomycin B, we also showed that RSG, apparently statically localized in the cytoplasm, is capable of shuttling in and out of the nucleus. These results suggest that 14-3-3 proteins negatively modulate RSG, which is involved in the regulation of endogenous amounts of GAs, by controlling its intracellular localization.