A conserved leucine zipper-like motif accounts for strong tetramerization capabilities of SEPALLATA-like MADS-domain transcription factors

Journal of Experimental Botany
Florian RümplerRainer Melzer

Abstract

The development of angiosperm flowers is regulated by homeotic MIKC-type MADS-domain transcription factors that activate or repress target genes via the formation of DNA-bound, organ-specific tetrameric complexes. The protein-protein interaction (PPI) capabilities differ considerably between different MIKC-type proteins. In Arabidopsis thaliana the floral homeotic protein SEPALLATA3 (SEP3) acts as a hub that incorporates numerous other MADS-domain proteins into tetrameric complexes that would otherwise not form. However, the molecular mechanisms that underlie these promiscuous interactions remain largely unknown. In this study, we created a collection of amino acid substitution mutants of SEP3 to quantify the contribution of individual residues on protein tetramerization during DNA-binding, employing methods of molecular biophysics. We show that leucine residues at certain key positions form a leucine-zipper structure that is essential for tetramerization of SEP3, whereas the introduction of physicochemically very similar residues at respective sites impedes the formation of DNA-bound tetramers. Comprehensive molecular evolutionary analyses of MADS-domain proteins from a diverse set of flowering plants revealed exceedingly high...Continue Reading

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Citations

Aug 2, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Xuelei LaiChloe Zubieta
Jul 22, 2020·Molecular Plant-microbe Interactions : MPMI·Marc-Benjamin AurinGünter Theißen
Apr 11, 2018·Journal of Experimental Botany·Veronique Hugouvieux, Chloe Zubieta
Jun 24, 2021·The Plant Journal : for Cell and Molecular Biology·Saraswati Nayar, Gokilavani Thangavel

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