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

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dc.contributor.authorPuranik, S.
dc.contributor.authorAcajjaoui, S.
dc.contributor.authorConn, S.
dc.contributor.authorCosta, L.
dc.contributor.authorConn, V.
dc.contributor.authorVial, A.
dc.contributor.authorMarcellin, R.
dc.contributor.authorMelzer, R.
dc.contributor.authorBrown, E.
dc.contributor.authorHart, D.
dc.contributor.authorTheiben, G.
dc.contributor.authorSilva, C.S.
dc.contributor.authorParcy, F.
dc.contributor.authorDumas, R.
dc.contributor.authorNanao, M.
dc.contributor.authorZubieta, C.
dc.date.issued2014
dc.descriptionData source: Supplemental data, http://www.plantcell.org.access.library.unisa.edu.au/content/26/9/3603/suppl/DC1
dc.description.abstractIn 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 floral meristem 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.
dc.identifier.citationThe Plant Cell, 2014; 26(9):3603-3615
dc.identifier.doi10.1105/tpc.114.127910
dc.identifier.issn1040-4651
dc.identifier.issn1532-298X
dc.identifier.urihttps://hdl.handle.net/1959.8/162157
dc.language.isoen
dc.publisherAmerican Society of Plant Biologists
dc.relation.fundingATIP-Avenir
dc.relation.fundingEU FP7 Contract BioStruct-X 283570
dc.relation.fundingEU FP7 Contract P-CUBE 227764
dc.relation.fundingFRISBI within the Grenoble Partnership for Structural Biology (PSB) ANR-10-INSB-05-02
dc.relation.fundingFRISBI ANR-10-INSB-05-02
dc.relation.fundingGRAL within the Grenoble Partnership for Structural Biology (PSB) ANR-10-LABX-49-01
dc.rightsCopyright 2014 American Society of Plant Biologists
dc.source.urihttps://doi.org/10.1105/tpc.114.127910
dc.subjecthomeotic genes
dc.subjectseed
dc.subjectplants
dc.titleStructural basis for the oligomerization of the MADS domain transcription factor SEPALLATA3 in Arabidopsis
dc.typeJournal article
pubs.publication-statusPublished
ror.mmsid9915914038101831

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