Structural basis for the oligomerization of the MADS domain transcription factor SEPALLATA3 in Arabidopsis

Sriharsha Purankik, Samira Acajjaoui, Simon Conn, Luca Costa, Vanessa Conn, Anthony Vial, Romain Marcellin, Rainer Melzer, Elizabeth Brown, Darren Hart, Gunter Theiben, Catarina Silva, Francois Parcy, Renaud Dumas, Max Nanao, Chloe Zubieta

    Research output: Contribution to journalArticlepeer-review

    73 Citations (Scopus)


    In plants, MADS domain transcription factors act as central regulators of diverse developmental pathways. In Arabidopsis thaliana, one of the most central members of this family is SEPALLATA3 (SEP3), which is involved in many aspects of plant reproduction, including floralmeristem and floral organ development. SEP3 has been shown to form homo and heterooligomeric complexes with other MADS domain transcription factors through its intervening (I) and keratin-like (K) domains. SEP3 function depends on its ability to form specific protein-protein complexes; however, the atomic level determinants of oligomerization are poorly understood. Here, we report the 2.5-Å crystal structure of a small portion of the intervening and the complete keratin-like domain of SEP3. The domains form two amphipathic alpha helices separated by a rigid kink, which prevents intramolecular association and presents separate dimerization and tetramerization interfaces comprising predominantly hydrophobic patches. Mutations to the tetramerization interface demonstrate the importance of highly conserved hydrophobic residues for tetramer stability. Atomic force microscopy was used to show SEP3-DNA interactions and the role of oligomerization in DNA binding and conformation. Based on these data, the oligomerization patterns of the larger family of MADS domain transcription factors can be predicted and manipulated based on the primary sequence.

    Original languageEnglish
    Pages (from-to)3603-3615
    Number of pages13
    JournalPlant Cell
    Issue number9
    Publication statusPublished - 1 Sept 2014


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