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THE PLANT CELL, Vol 8, Issue 1 81-94, Copyright © 1996 by American Society of Plant Biologists

RESEARCH ARTICLES

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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