Arabidopsis FHY1 protein stability is regulated by light via phytochrome A and 26S proteasome. Export

@article{citeulike:4222251, abstract = {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 down-regulated during further seedling development and by light exposure. By using light-insensitive 35S promoter-driven functional beta-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.}, author = {Shen, Y. and Feng, S. and Ma, L. and Lin, R. and Qu, L. J. and Chen, Z. and Wang, H. and Deng, X. W.}, citeulike-article-id = {4222251}, citeulike-linkout-0 = {http://dx.doi.org/10.1104/pp.105.067645}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16244150}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16244150}, doi = {10.1104/pp.105.067645}, issn = {0032-0889}, journal = {Plant physiology}, keywords = {fhy1, phya, proteasome}, month = {November}, number = {3}, pages = {1234--1243}, posted-at = {2009-03-26 14:41:01}, priority = {2}, title = {Arabidopsis FHY1 protein stability is regulated by light via phytochrome A and 26S proteasome.}, url = {http://dx.doi.org/10.1104/pp.105.067645}, volume = {139}, year = {2005} }

TY - JOUR ID - citeulike:4222251 L3 - citeulike-article-id:4222251 N2 - 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 down-regulated during further seedling development and by light exposure. By using light-insensitive 35S promoter-driven functional beta-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. IS - 3 JF - Plant physiology SN - 0032-0889 EP - 1243 TI - Arabidopsis FHY1 protein stability is regulated by light via phytochrome A and 26S proteasome. VL - 139 SP - 1234 KW - fhy1 KW - phya KW - proteasome AU - Shen, Y AU - Feng, S AU - Ma, L AU - Lin, R AU - Qu, LJ AU - Chen, Z AU - Wang, H AU - Deng, XW PY - 2005/11// UR - http://dx.doi.org/10.1104/pp.105.067645 ER -