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Plant and Cell Physiology Advance Access published online on July 28, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci178
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Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received April 15, 2005
Accepted July 23, 2005

Regular Paper

LIP19, a Basic Region Leucine Zipper Protein, Is a Fos-like Molecular Switch in the Cold Signaling of Rice Plants

Hidekazu Shimizu 1 4, Kazuhito Sato 1 4, Thomas Berberich 2, Atsushi Miyazaki 1, Rei Ozaki 1, Ryozo Imai 3, and Tomonobu Kusano 1*

1 Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan
2 Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan; Botanisches Institut, Goethe-Universität, Postfach 11 19 32, D-60054, Frankfurt am Main, Germany
3 Winter Stress Laboratory, National Agricultural Research Center for Hokkaido Region, Hitsujigaoka 1, Toyohira-ku, Sapporo 062-8555, Japan

* To whom correspondence should be addressed.
Tomonobu Kusano, E-mail: kusano{at}ige.tohoku.ac.jp


  Abstract

Rice low-temperature-induced lip19 gene encodes a 148 amino acid basic region/leucine zipper (bZIP) protein, termed LIP19. Here we characterized LIP19 and showed that it lacks the usual ability of bZIP proteins to homodimerize and to bind DNA, similar to the Fos protein in mammals. Using a yeast two-hybrid system, the cDNA clones whose products interact with LIP19 were screened. This search revealed a clone termed OsOBF1 (Oryza sativa OBF1) that encodes a new bZIP protein (OsOBF1). This protein forms a homodimer and binds to the hexamer motif sequence (5'-ACGTCA-3'). The protein-protein interaction in homo- and hetero-combinations between LIP19 and OsOBF1 was confirmed in vitro and in planta. LIP19 and OsOBF1 most likely interact with each other more strongly than OsOBF1 interacts with itself, and the resulting heterodimer binds to the C/G hybrid sequence but not to the hexamer sequence. Whereas the expression patterns of lip19 and OsOBF1 in response to low temperatures were totally opposite, the locations of their expression were almost identical. Based upon the presented data, we propose a model describing the low-temperature signal switching mediated by LIP19 in rice.

Keywords: bZIP protein; cold signaling; DNA binding; heterodimer; molecular switch; rice.

4 These two authors contributed equally to this work


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