The intervening domain is required for DNA-binding and functional identity of plant MADS transcription factors

Xuelei Lai, Rosario Vega-Léon, Veronique Hugouvieux (), Romain Blanc-Mathieu, Froukje Wal, Jérémy Lucas, Catarina S. Silva, Agnès Jourdain, Jose M. Muino, Max H. Nanao, Richard Immink, Kerstin Kaufmann, François Parcy, Cezary Smaczniak () and Chloe Zubieta ()
Additional contact information
Xuelei Lai: Université Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV
Rosario Vega-Léon: Humboldt-Universität zu Berlin
Veronique Hugouvieux: Université Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV
Romain Blanc-Mathieu: Université Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV
Froukje Wal: Wageningen University and Research
Jérémy Lucas: Université Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV
Catarina S. Silva: Université Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV
Agnès Jourdain: Université Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV
Jose M. Muino: Humboldt-Universität zu Berlin
Max H. Nanao: Structural Biology Group
Richard Immink: Wageningen University and Research
Kerstin Kaufmann: Humboldt-Universität zu Berlin
François Parcy: Université Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV
Cezary Smaczniak: Humboldt-Universität zu Berlin
Chloe Zubieta: Université Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: Abstract The MADS transcription factors (TF) are an ancient eukaryotic protein family. In plants, the family is divided into two main lineages. Here, we demonstrate that DNA binding in both lineages absolutely requires a short amino acid sequence C-terminal to the MADS domain (M domain) called the Intervening domain (I domain) that was previously defined only in type II lineage MADS. Structural elucidation of the MI domains from the floral regulator, SEPALLATA3 (SEP3), shows a conserved fold with the I domain acting to stabilise the M domain. Using the floral organ identity MADS TFs, SEP3, APETALA1 (AP1) and AGAMOUS (AG), domain swapping demonstrate that the I domain alters genome-wide DNA-binding specificity and dimerisation specificity. Introducing AG carrying the I domain of AP1 in the Arabidopsis ap1 mutant resulted in strong complementation and restoration of first and second whorl organs. Taken together, these data demonstrate that the I domain acts as an integral part of the DNA-binding domain and significantly contributes to the functional identity of the MADS TF.

Date: 2021
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DOI: 10.1038/s41467-021-24978-w

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