Molecular cloning and characterization of OsUPS,a U-box containing E3 ligase gene that respond to phosphate starvation in rice (<Emphasis Type="Italic">Oryza sativa</Emphasis>) |
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Authors: | Yeon-Jae Hur Young Byung Yi Jai Heon Lee Young Soo Chung Ho Won Jung Dae Jin Yun Kyung-Min Kim Dong Soo Park Doh Hoon Kim |
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Institution: | (1) College of Life Science and Natural Resources, Dong-A University, Busan, 604-714, Korea;(2) Division of Applied Life Science, Gyeongsang National University, Jinju, 660-701, Korea;(3) College of Ecology and Environmental Science, Kyungpook National University, Sangju, 742-711, Korea;(4) Department of Functional Crop, National Institute of Crop Science, RDA, Milyang, 627-803, Korea; |
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Abstract: | The ubiquitin-26S proteasome system is important in the quality control of intracellular proteins. The ubiquitin-26S proteasome
system includes the E1 (ubiquitin activating), E2 (ubiquitin conjugating), and E3 (ubiquitin ligase) enzymes. U-box proteins
are a derived version of RING-finger domains, which have E3 enzyme activity. Here, we present the isolation of a novel U-box
protein, U-box containing E3 ligase induced by phosphate starvation (OsUPS), from rice (Oryza sativa). The cDNA encoding the O. sativa U-box protein (OsUPS) comprises 1338 bp, with an open reading frame of 445 amino acids. The amino acid sequence of OsUPS
cDNA shows 41–79% identity with other plant U-box homologous genes. The open reading frame of the OsUPS protein is comprised
of notable domains: a single ~70-amino acid domain and a GKL domain that contains conserved glycine, lysine/arginine residues
and leucine-rich feature. We found that full-length expression of OsUPS was up-regulated in both rice plants and cell culture
in the absence of inorganic phosphate (Pi). A self-ubiquitination assay indicated that the bacterially expressed OsUPS protein had E3 ligase activity, and subcellular
localization results showed that OsUPS was located in the chloroplast. These results support the notion that OsUPS plays an
important role in the Pi signaling pathway through the ubiquitin-26S proteasome system. |
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