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THE PLANT CELL, Vol 8, Issue 1 81-94, Copyright © 1996 by American Society of Plant Biologists
DNA Binding Properties of Two Arabidopsis MADS Domain Proteins: Binding Consensus and Dimer Formation
H. Huang, M. Tudor, T. Su, Y. Zhang, Y. Hu and H. Ma
Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, New York 11724-2212
MADS domain proteins are members of a highly conserved family found in all
eukaryotes. Genetic studies clearly indicate that many plant MADS domain
proteins have different regulatory functions in flower development, yet
they share a highly conserved DNA binding domain and can bind to very
similar sequences. How, then, can these MADS box genes confer their
specific functions? Here, we describe results from DNA binding studies of
AGL1 and AGL2 (for AGAMOUS-like), two Arabidopsis MADS domain proteins that
are preferentially expressed in flowers. We demonstrate that both proteins
are sequence-specific DNA binding proteins and show that each binding
consensus has distinct features, suggesting a mechanism for specificity. In
addition, we show that the proteins with more similar amino acid sequences
have more similar binding sequences. We also found that AGL2 binds to DNA
in vitro as a dimer and determined the region of AGL2 that is sufficient
for DNA binding and dimerization. Finally, we show that several plant MADS
domain proteins can bind to DNA either as homodimers or as heterodimers,
suggesting that the number of different regulators could be much greater
than the number of MADS box genes.
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