| Literature DB >> 12671091 |
Jan Smalle1, Jasmina Kurepa, Peizhen Yang, Thomas J Emborg, Elena Babiychuk, Sergei Kushnir, Richard D Vierstra.
Abstract
The 26S proteasome is an essential protease complex responsible for removing most short-lived intracellular proteins, especially those modified with polyubiquitin chains. We show here that an Arabidopsis mutant expressing an altered RPN10 subunit exhibited a pleiotropic phenotype consistent with specific changes in 26S proteasome function. rpn10-1 plants displayed reduced seed germination, growth rate, stamen number, genetic transmission through the male gamete, and hormone-induced cell division, which can be explained partially by a constitutive downregulation of the key cell cycle gene CDKA;1. rpn10-1 also was more sensitive to abscisic acid (ABA), salt, and sucrose stress and to DNA-damaging agents and had decreased sensitivity to cytokinin and auxin. Most of the phenotypes can be explained by a hypersensitivity to ABA, which is reflected at the molecular level by the selective stabilization of the short-lived ABA-signaling protein ABI5. Collectively, these results indicate that RPN10 affects a number of regulatory processes in Arabidopsis likely by directing specific proteins to the 26S proteasome for degradation. A particularly important role may be in regulating the responses to signals promulgated by ABA.Entities:
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Year: 2003 PMID: 12671091 PMCID: PMC152342 DOI: 10.1105/tpc.009217
Source DB: PubMed Journal: Plant Cell ISSN: 1040-4651 Impact factor: 11.277