ArticleJournal of experimental botany2014
Post-translational regulation of rice MADS29 function: homodimerization or binary interactions with other seed-expressed MADS proteins modulate its translocation into the nucleus.
Article in Journal of experimental botany, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 35 citations in OpenAlex.
- The OsMADS18-OsbZIP60 module plays a critical role in influencing grain chalkiness in rice.Science China. Life sciences · 2026Article
- Let go or retain: role of calmodulin in orchestrating nuclear protein transport in eukaryotes.Plant cell reports · 2026Review
- Phenotyping analysis of rice cv. Nipponbare overexpressing OsMADS56 gene in drought tolerance, plant height, and yield components.Journal, genetic engineering & biotechnology · 2025Article
- MADS31 supports female germline development by repressing the post-fertilization programme in cereal ovules.Nature plants · 2025Article
- MIKC-type MADS-box transcription factor OsMADS31 positively regulates salinity tolerance in rice.Frontiers in plant science · 2025Article
- Upstream regulator of genomic imprinting in rice endosperm is a small RNA-associated chromatin remodeler.Nature communications · 2024Article
- Antagonistic regulation of target genes by the SISTER OF TM3-JOINTLESS2 complex in tomato inflorescence branching.The Plant cell · 2023Article
- Article
- Characterization of Transcription Regulatory Domains of OsMADS29: Identification of Proximal Auxin-Responsive Domains and a Strong Distal Negative Element.Frontiers in plant science · 2022Article
- A MADS-Box GeneInternational journal of molecular sciences · 2021Article
- Orchid BScientific reports · 2021Article
- A Gas-and-Brake Mechanism of bHLH Proteins Modulates Shade Avoidance.Plant physiology · 2020Article
- Article
- Analysis of rice nuclear-localized seed-expressed proteins and their database (RSNP-DB).Scientific reports · 2020Article
- Exploring the Role of a Cytokinin-Activating Enzyme LONELY GUY in Unicellular MicroalgaFrontiers in plant science · 2020Article
- OsMADS18, a membrane-bound MADS-box transcription factor, modulates plant architecture and the abscisic acid response in rice.Journal of experimental botany · 2019Article
- Suppression of OsMADS7 in rice endosperm stabilizes amylose content under high temperature stress.Plant biotechnology journal · 2018Article
- Rice Improvement Through Genome-Based Functional Analysis and Molecular Breeding in India.Rice (New York, N.Y.) · 2016Article
- Feedback Regulation of DYT1 by Interactions with Downstream bHLH Factors Promotes DYT1 Nuclear Localization and Anther Development.The Plant cell · 2016Article
- Three Rice NAC Transcription Factors Heteromerize and Are Associated with Seed Size.Frontiers in plant science · 2016Article
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3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
OsMADS29 is a seed-specific MADS-box transcription factor that affects embryo development and grain filling by maintaining hormone homeostasis and degradation of cells in the nucellus and nucellar projection. Although it has a bipartite nuclear localization signal (NLS) sequence, the transiently expressed OsMADS29 monomer does not localize specifically in the nucleus. Dimerization of the monomers alters the intracellular localization fate of the resulting OsMADS29 homodimer, which then translocates into the nucleus. By generating domain-specific deletions/mutations, we show that two conserved amino acids (lysine(23) and arginine(24)) in the NLS are important for nuclear localization of the OsMADS29 homodimer. Furthermore, the analyses involving interaction of OsMADS29 with 30 seed-expressed rice MADS proteins revealed 19 more MADS-box proteins, including five E-class proteins, which interacted with OsMADS29. Eleven of these complexes were observed to be localized in the nucleus. Deletion analysis revealed that the KC region (K-box and C-terminal domain) plays a pivotal role in homodimerization. These data suggest that the biological function of OsMADS29 may not only be regulated at the level of transcription and translation as reported earlier, but also at the post-translational level by way of the interaction between OsMADS29 monomers, and between OsMADS29 and other MADS-box proteins.
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