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Characterization of a novel rice bZIP protein which binds to the α-globulin promoter

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Abstract

Many plant basic leucine-zipper (bZIP) proteins have been isolated several of which have been shown to play a role in seed-specific gene expression. We isolated a novel bZIP protein (REB) gene encoding 425 amino acid residues from rice endosperm, which is similar to Opaque-2 heterodimerizing protein (OHP) of maize. The gene product, termed REB, contains Pro- and Gly-rich regions at its N terminus, followed by the typical basic and leucine-repeat regions. Recombinant REB binds to the region from -754 to -562 in the α-globulin gene promoter, but not to promoters of other major storage genes such as glutelin, prolamin and albumin. The 5′ region of the α-globulin gene possesses three binding sites for REB, which were determined as GCCACGT(A/C)AG, by using synthetic oligonucleotides. A Super-shift assay using anti-REB antibody suggested that REB is a major DNA-binding protein for the α-globulin gene promoter in rice endosperm.

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Authors and Affiliations

  1. Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University, Chikusa-ku, Nagoya, 464-01, Japan

    Masayuki Nakase, Naohito Aoki, Tsukasa Matsuda & Takahiro Adachi

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  1. Masayuki Nakase
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  2. Naohito Aoki
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  3. Tsukasa Matsuda
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  4. Takahiro Adachi
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Nakase, M., Aoki, N., Matsuda, T. et al. Characterization of a novel rice bZIP protein which binds to the α-globulin promoter. Plant Mol Biol 33, 513–522 (1997). https://doi.org/10.1023/A:1005784717782

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