Plant and Cell Physiology Advance Access originally published online on July 28, 2005
Plant and Cell Physiology 2005 46(10):1623-1634; doi:10.1093/pcp/pci178
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LIP19, a Basic Region Leucine Zipper Protein, is a Fos-like Molecular Switch in the Cold Signaling of Rice Plants
1 Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi, 980-8577 Japan
2 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
* Corresponding author: E-mail, kusano{at}ige.tohoku.ac.jp; Fax, +81-22-217-5709.
The rice low-temperature-induced lip19 gene encodes a 148-amino-acid basic region/leucine zipper (bZIP) protein, termed LIP19. In this study we characterized LIP19 and showed that it lacks the usual ability of bZIP proteins to homodimerize and to bind DNA, as does 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 proteinprotein 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.
The nucleotide sequence reported in this paper has been submitted to DDBJ under accession No. AB185280 [GenBank] (OsOBF1).
4 These two authors contributed equally to this work.
(Received April 15, 2005; Accepted July 23, 2005)
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