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First published online July 18, 2002; 10.1105/tpc.001735

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The Plant Cell, Vol. 14, 1963-1980, August 2002, Copyright © 2002,
American Society of Plant Biologists

Three Novel MYB Proteins with One DNA Binding Repeat Mediate Sugar and Hormone Regulation of {alpha}-Amylase Gene Expression

Chung-An Lua, Tuan-hua David Hob, Shin-Lon Ho1,a and Su-May Yu2,a

a Institute of Molecular Biology, Academia Sinica, Nankang, Taipei, Taiwan 115, Republic of China
b Department of Biology, Washington University, St. Louis, Missouri 63130

2 To whom correspondence should be addressed. E-mail sumay{at}ccvax.sinica.edu.tw; fax 886-2-2788-2695

The expression of {alpha}-amylase genes in cereals is induced by both gibberellin (GA) and sugar starvation. All {alpha}-amylase genes isolated from cereals contain a TATCCA element or its variants at positions ~90 to 150 bp upstream of the transcription start sites. The TATCCA element was shown previously to be an important component of the GA response complex and the sugar response complex of {alpha}-amylase gene promoters. In the present study, three cDNA clones encoding novel MYB proteins with single DNA binding domains were isolated from a rice suspension cell cDNA library and designated OsMYBS1, OsMYBS2, and OsMYBS3. Gel mobility shift experiments with OsMYBSs showed that they bind specifically to the TATCCA element in vitro. Yeast one-hybrid experiments demonstrated that OsMYBS1 and OsMYBS2 bind to the TATCCA element and transactivate a promoter containing the TATCCA element in vivo. Transient expression assays with barley half-seeds showed that OsMYBS1 and OsMYBS2 transactivate a promoter containing the TATCCA element when sugar is provided, whereas OsMYBS3 represses transcription of the same promoter under sugar starvation. Transient expression assays also showed that these three OsMYBSs cooperate with a GA-regulated transcription factor, HvMYBGa, in the transactivation of a low-pI barley {alpha}-amylase gene promoter in the absence of GA. Two-hybrid experiments with barley half-seeds showed that OsMYBS1 is able to form a homodimer. The present study demonstrates that differential DNA binding affinity, promoter transactivation ability, dimerization, and interactions with other protein factors determine the biological function of OsMYBSs. This study also suggests that common transcription factors are involved in the sugar and hormonal regulation of {alpha}-amylase gene expression in cereals.




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