Vega-Leon, R. | Search bioRxiv

bioRxiv2025

ARABIDOPSIS Bsister and SEEDSTICK MADS-box transcription factors modulate maternal nutrient flow for seed development in Arabidopsis

Successful seed development in angiosperms depends on the coordinated transport and allocation of sugars from maternal tissues to the developing embryo and endosperm. In Arabidopsis thaliana, ovules function as carbohydrate sink organs, accumulating starch in both gametophytic and sporophytic domains prior to fertilization. This stored starch is later mobilized to support early embryogenesis. Despite extensive knowledge of starch metabolism in photosynthetic tissues, the regulatory mechanisms governing sugar transport in reproductive organs remain poorly understood. Recent studies have identified fertilization-dependent changes in nutrient flow, including callose-mediated modulation of symplastic transport at the phloem unloading site. However, the molecular players orchestrating these transitions are largely unknown. Here, we show that the MIKC MADS domain transcription factors ABS/TT16 and STK play critical roles in regulating maternal nutrient flow during ovule maturation and seed development. We dissect their functional redundancy using omics and genetic approaches, underscoring the importance of different ovule tissues in coordinating sugar transport pathways for post-fertilization development. Our findings reveal a previously underappreciated layer of genetic control over nutrient allocation in reproductive tissues and provide new insights into the metabolic reprogramming required for successful seed formation.

plant biology↗

bioRxiv2021

The Intervening Domain Is Required For DNA-binding and Functional Identity of Plant MADS Transcription Factors

The MADS transcription factors (TF) are an ancient protein family with a high degree of sequence identity that bind almost identical DNA sequences across all eukaryotic kingdoms of life, yet fulfill dramatically different physiological roles. In plants, the family is divided into two main lineages, type I and II, based on sequence conservation of the DNA-binding MADS-box domain (M domain) with yeast and animal M domains. Here, we demonstrate that DNA binding in both lineages absolutely requires a short amino acid sequence C-terminal to the M domain called the Intervening domain (I domain) in type II MADS. Structural elucidation of the MI domains from the floral regulator, SEPALLATA3 (SEP3), shows a highly conserved MADS-box fold with the I domain forming an alpha helix and acting to stabilize the M domain. Based on secondary structure prediction, sequences fulfilling the same function as the SEP3 I domain can be found in both lineages of plant MADS TFs, suggesting the I domain is a conserved and required part of the DNA-binding domain. Using the floral organ identity MADS TFs, SEP3, APETALA1 (AP1) and AGAMOUS (AG), domain swapping demonstrate that the I domain alters DNA-binding specificity based on seq-DAP-seq experiments. Yeast 2-hybrid experiments further revealed the role of the I domain in dimerization specificity. Surprisingly, introducing AG carrying the I domain of AP1 in the Arabidopsis ap1 mutant, resulted in a high degree of complementation and restoration of first and second whorl organs. Taken together, these data demonstrate that the I domain acts both as an integral part of the DNA-binding domain and strongly contributes to the functional identity of the MADS TF.

plant biology↗