ArticleThe Plant cell2014
Structural basis for the oligomerization of the MADS domain transcription factor SEPALLATA3 in Arabidopsis.
Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed.
- The phytoplasma effector, phyllogen, structurally mimics host plant MADS transcription factors.The Journal of biological chemistry · 2026Article
- Alphafuser: a parsimonious approach to predicting higher-order protein complexes.Acta crystallographica. Section D, Structural biology · 2026Article
- Article
- Phylogenomic profile of exon-intron organization across angiosperms, their relationships with protein domains, and functional implications.Nature communications · 2026Article
- Utilization of MADS-Box genes for agricultural advancement: current insights and future prospects.Molecular biology reports · 2025Review
- The origin, evolution, and diversification of MADS-box transcription factors in green plants.Plant communications · 2025Article
- Genome-wide characterization and expression profiling of MADS-box family genes during organ development and drought stress in Camelina sativa L.Scientific reports · 2025Article
- Identification, expression analyses ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2025Article
- Article
- A regulatory module mediating temperature control of cell-cell communication facilitates tree bud dormancy release.The EMBO journal · 2024Article
- Uncoupling FRUITFULL's functions through modification of a protein motif identified by co-ortholog analysis.Nucleic acids research · 2024Article
- Single nucleotide polymorphisms in SEPALLATA 2 underlie fruit length variation in cucurbits.The Plant cell · 2024Article
- SEPALLATA-driven MADS transcription factor tetramerization is required for inner whorl floral organ development.The Plant cell · 2024Article
- Genome-wide identification and expression pattern analysis of MIKC-Type MADS-box genes in Chionanthus retusus, an androdioecy plant.BMC genomics · 2024Article
- Reflections on the ABC model of flower development.The Plant cell · 2024Review
- Dynamic evolution of MADS-box genes in extant ferns via large-scale phylogenomic analysis.Frontiers in plant science · 2024Article
- Regulation of micro- and small-exon retention and other splicing processes by GRP20 for flower development.Nature plants · 2024Article
- Genome-wide analysis of the MADS-box gene family in Lonicera japonica and a proposed floral organ identity model.BMC genomics · 2023Article
- One pattern analysis (OPA) for the quantitative determination of protein interactions in plant cells.Plant methods · 2023Article
- Article
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16 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In 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.
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