LIP19, a basic region leucine zipper protein, is a fos-like molecular switch in the cold signaling of rice plants

Hidekazu Shimizu, Kazuhito Sato, Thomas Berberich, Atsushi Miyazaki, Rei Ozaki, Ryozo Imai, Tomonobu Kusano

    Research output: Contribution to journalArticlepeer-review

    72 Citations (Scopus)


    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 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. JSPP

    Original languageEnglish
    Pages (from-to)1623-1634
    Number of pages12
    JournalPlant and Cell Physiology
    Issue number10
    Publication statusPublished - 2005 Oct


    • Cold signaling
    • DNA binding
    • Heterodimer
    • Molecular switch
    • Rice
    • bZIP protein

    ASJC Scopus subject areas

    • Physiology
    • Plant Science
    • Cell Biology

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