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

Characterization of a novel rice bZIP protein which binds to the α-globulin promoter 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. Plant Molecular Biology Springer Journals

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

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Kluwer Academic Publishers
Copyright © 1997 by Kluwer Academic Publishers
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
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