DNA binding properties of two Arabidopsis MADS domain proteins: Binding consensus and dimer formation

Hai Huang, Matthew Tudor, Thomas Su, Yue Zhang, Yi Hu, Hong Ma

Research output: Contribution to journalArticlepeer-review

111 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)81-94
Number of pages14
JournalPlant Cell
Volume8
Issue number1
DOIs
StatePublished - Jan 1996

All Science Journal Classification (ASJC) codes

  • Plant Science
  • Cell Biology

Fingerprint Dive into the research topics of 'DNA binding properties of two Arabidopsis MADS domain proteins: Binding consensus and dimer formation'. Together they form a unique fingerprint.

Cite this