ArticlePlant physiology1999
Determination of the motif responsible for interaction between the rice APETALA1/AGAMOUS-LIKE9 family proteins using a yeast two-hybrid system.
Article in Plant physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 149 citations in OpenAlex.
- The OsMADS18-OsbZIP60 module plays a critical role in influencing grain chalkiness in rice.Science China. Life sciences · 2026Article
- Natural variation in OsMADS1 transcript splicing affects rice grain thickness and quality by influencing monosaccharide loading to the endosperm.Plant communications · 2025Article
- Functional characterization ofFrontiers in plant science · 2025Article
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2023Article
- The ABC of Flower Development in Monocots: The Model of Rice Spikelet.Methods in molecular biology (Clifton, N.J.) · 2023Article
- BabyBoom: 3-Dimensional Structure-Based Ligand and Protein Interaction Prediction by Molecular Docking.Biomolecules · 2022Article
- A homologous gene of OsREL2/ASP1, ASP-LSL regulates pleiotropic phenotype including long sterile lemma in rice.BMC plant biology · 2021Article
- Alternatively splicedHorticulture research · 2020Article
- OsMADS18, a membrane-bound MADS-box transcription factor, modulates plant architecture and the abscisic acid response in rice.Journal of experimental botany · 2019Article
- Article
- Loss of LOFSEP Transcription Factor Function Converts Spikelet to Leaf-Like Structures in Rice.Plant physiology · 2018Article
- Article
- Homodimerization of Ehd1 Is Required to Induce Flowering in Rice.Plant physiology · 2016Article
- Down-regulation of a LBD-like gene, OsIG1, leads to occurrence of unusual double ovules and developmental abnormalities of various floral organs and megagametophyte in rice.Journal of experimental botany · 2015Article
- Post-translational regulation of rice MADS29 function: homodimerization or binary interactions with other seed-expressed MADS proteins modulate its translocation into the nucleus.Journal of experimental botany · 2014Article
- Evolution of fruit development genes in flowering plants.Frontiers in plant science · 2014Article
- Ectopic expression of OsMADS45 activates the upstream genes Hd3a and RFT1 at an early development stage causing early flowering in rice.Botanical studies · 2013Article
- Fine mapping of BH1, a gene controlling lemma and palea development in rice.Plant cell reports · 2013Article
- Assessing duplication and loss of APETALA1/FRUITFULL homologs in Ranunculales.Frontiers in plant science · 2013Article
- Expression dynamics of metabolic and regulatory components across stages of panicle and seed development in indica rice.Functional & integrative genomics · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A MADS family gene, OsMADS6, was isolated from a rice (Oryza sativa L.) young flower cDNA library using OsAMDS1 as a probe. With this clone, various MADS box genes that encode for protein-to-protein interaction partners of the OsMADS6 protein were isolated by the yeast two-hybrid screening method. On the basis of sequence homology, OsMADS6 and the selected partners can be classified in the APETALA1/AGAMOUS-LIKE9 (AP1/AGL9) family. One of the interaction partners, OsMADS14, was selected for further study. Both genes began expression at early stages of flower development, and their expression was extended into the later stages. In mature flowers the OsMADS6 transcript was detectable in lodicules and also weakly in sterile lemmas and carpels, whereas the OsMADS14 transcript was detectable in sterile lemmas, paleas/lemmas, stamens, and carpels. Using the yeast two-hybrid system, we demonstrated that the region containing of the 109th to 137th amino acid residues of OsMADS6 is indispensable in the interaction with OsMADS14. Site-directed mutation analysis revealed that the four periodical leucine residues within the region are essential for this interaction. Furthermore, it was shown that the 14 amino acid residues located immediately downstream of the K domain enhance the interaction, and that the two leucine residues within this region play an important role in that enhancement.
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