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期刊论文

Arabidopsis FHY1 Protein Stability Is Regulated by Lightvia Phytochrome A and 26S Proteasome1

马力耕Yunping Shen Suhua Feng Ligeng Ma Rongcheng Lin Li-Jia Qu Zhangliang Chen Haiyang Wang and Xing Wang Deng*

Plant Physiology, November 2005, Vol. 139, pp. 1234-1243,-0001,():

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摘要/描述

Phytochrome A (phyA) is the primary photoreceptor mediating responses to far-red light. Among the phyA downstream signaling components, Far-red Elongated Hypocotyl 1 (FHY1) is a genetically defined positive regulator of photomorphogenesis in far-red light. Both physiological and genomic characterization of the fhy1 mutants indicated a close functional relationship of FHY1 with phyA. Here, we showed that FHY1 is most abundant in young seedlings grown in darkness and is quickly downregulated during further seedling development and by light exposure. By using light-insensitive 35S promoter-driven functional β-glucuronidase-FHY1 and green fluorescent protein-FHY1 fusion proteins, we showed that this down-regulation of FHY1 protein abundance by light is largely at posttranscriptional level and most evident in the nuclei. The light-triggered FHY1 protein reduction is primarily mediated through the 26S proteasome-dependent protein degradation. Further, phyA is directly involved in mediating the light-triggered down-regulation of FHY1, and the dark accumulation of FHY1 requires functional pleiotropic Constitutive Photomorphogenic/De-Etiolated/Fusca proteins. Our data indicate that phyA, the 26S proteasome, and the Constitutive Photomorphogenic/De-Etiolated/Fusca proteins are all involved in the light regulation of FHY1 protein abundance during Arabidopsis (Arabidopsis thaliana) seedling development.

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