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Plant and Cell Physiology, 2002, Vol. 43, No. 5 532-539
© 2002 Oxford University Press

Isolation and Characterization of a Putative Transducer of Endoplasmic Reticulum Stress in Oryza sativa

Yoko Okushima1, Nozomu Koizumi2, Yube Yamaguchi, Yukio Kimata, Kenji Kohno and Hiroshi Sano

Research and Education Center for Genetic Information, Nara Institute of Science and Technology, Ikoma, 630-0101 Japan

Following endoplasmic reticulum (ER) stress that prevents correct folding or assembly of ER proteins, at least three responses occur to maintain cell homeostasis: induction of chaperones, attenuation of protein synthesis, and enhancement of lipid synthesis. Transducers that transmit ER stress to the nucleus have already been identified in yeast and mammals. We report here isolation of a cDNA, OsIre1, from rice encoding a putative homolog of Ire1p, a yeast transducer of ER stress. OsIre1 encodes a polypeptide consisting of 893 amino acids, in which two hydrophobic stretches are present in the amino-terminal (N-terminal) and middle regions, possibly serving as a signal peptide and a transmembrane domain, respectively. The carboxyl-terminal (C-terminal) domain was found to possess serine/threonine protein kinase and ribonuclease-like domains showing high similarities with regions in Ire1 homologs from other organisms. A fusion protein of OsIre1 and green fluorescent protein (GFP) expressed in tobacco BY2 cells could be demonstrated to localize to the ER and the N-terminal domain of OsIre1 could substitute for yeast Ire1p in yeast cells. When produced in bacteria as a fusion protein, the C-terminal region of OsIre1 showed autophosphorylation activity. These results thus indicate that OsIre1 encodes a putative plant transducer of ER stress.

1 Present address: Plant Gene Expression Center, University of California Berkeley, 800 Buchanan Street, Albany, CA 94710, U.S.A.

2 Corresponding author: E-mail, nkoizumi@gtc.aist-nara.ac.jp; Fax, +81-743-72-5659.


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