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THE PLANT CELL, Vol 9, Issue 2 171-184, Copyright © 1997 by American Society of Plant Biologists
The Wheat Transcriptional Activator SPA: A Seed-Specific bZIP Protein That Recognizes the GCN4-like Motif in the Bifactorial Endosperm Box of Prolamin Genes
D. Albani, MCU. Hammond-Kosack, C. Smith, S. Conlan, V. Colot, M. Holdsworth and M. W. Bevan
Molecular Genetics Department, John Innes Centre, Colney Lane, Norwich NR4 7UJ, United Kingdom
The conserved bifactorial endosperm box found in the promoter of wheat
storage protein genes comprises two different cis elements that are thought
to be involved in regulating endosperm-specific gene expression. Endosperm
nuclear extracts contain binding activities. One is called ESBF-I, which
binds to the endosperm motif (EM), and the other is called ESBF-II, which
binds to the GCN4-like motif (GLM). Here, we present a functional analysis
of the endosperm box of a low-molecular-weight glutenin gene found on the
1D1 chromosome of hexaploid wheat (LMWG-1D1) in transgenic tobacco plants.
Our analysis demonstrates the necessity of the EM and GLM for
endosperm-specific gene expression and suggests the presence in tobacco of
functional counterparts of wheat ESBF-I and ESBF-II. Furthermore, we
describe the isolation and characterization of cDNA clones encoding SPA, a
seed-specific basic leucine zipper protein from wheat that can activate
transcription from the GLMs of the -326-bp LMWG-1D1 promoter in both maize
and tobacco leaf protoplasts. This activation is also partially dependent
on the presence of functional EMs, suggesting interactions between SPA with
ESBF-I-like activities.
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