Uncoupling FRUITFULL’s Functions Through Modification of a Protein Motif Identified by Co-Ortholog Analysis

Kai Thoris,Miguel Correa Marrero,Martijn Fiers,Xuelei Lai,Iris E. Zahn,Xiaobing Jiang,Mark Mekken, Stefan Busscher, Stuart Jansma,Max Nanao,Dick de Ridder,Aalt D. J. van Dijk,Gerco C. Angenent,Richard G. H. Immink,Chloe Zubieta,Marian Bemer

Nucleic acids research（2024）

Wageningen Univ & Res

Cited 0|Views4

Abstract

Many plant transcription factors (TFs) are multifunctional and regulate growth and development in more than one tissue. These TFs can generally associate with different protein partners depending on the tissue type, thereby regulating tissue-specific target gene sets. However, how interaction specificity is ensured is still largely unclear. Here, we examine protein-protein interaction specificity using subfunctionalized co-orthologs of the FRUITFULL (FUL) subfamily of MADS-domain TFs. In Arabidopsis, FUL is multifunctional, playing important roles in flowering and fruiting, whereas these functions have partially been divided in the tomato co-orthologs FUL1 and FUL2. By linking protein sequence and function, we discovered a key amino acid motif that determines interaction specificity of MADS-domain TFs, which in Arabidopsis FUL determines the interaction with AGAMOUS and SEPALLATA proteins, linked to the regulation of a subset of targets. This insight offers great opportunities to dissect the biological functions of multifunctional MADS TFs.

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