SULFORHODAMINE 101_PEO2_PROPIONIC ACID S
- Known as:
- SULFORHODAMINE 101_PEO2_PROPIONIC ACID S
- Catalog number:
- 90039
- Product Quantity:
- 5 MG
- Category:
- -
- Supplier:
- Biotium
- Gene target:
- SULFORHODAMINE 101_PEO2_PROPIONIC ACID
Related genes to: SULFORHODAMINE 101_PEO2_PROPIONIC ACID S
- Gene:
- MED25 NIH gene
- Name:
- mediator complex subunit 25
- Previous symbol:
- -
- Synonyms:
- ARC92, ACID1, TCBAP0758, DKFZp434K0512
- Chromosome:
- 19q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-11-09
- Date modifiied:
- 2019-04-23
Related products to: SULFORHODAMINE 101_PEO2_PROPIONIC ACID S
Related articles to: SULFORHODAMINE 101_PEO2_PROPIONIC ACID S
- In canonical jasmonate (JA) signaling, MYC2 activity is restrained by JA-inducible JAZ repressors that are rapidly degraded upon JA perception. However, it remains unclear how MYC2 is attenuated during prolonged developmental processes such as leaf senescence, where sustained repression is required independently of acute JA fluctuations. Here, we identify C-type cyclin 1;1 (CycC1;1) as a negative regulator of JA-induced leaf senescence in Arabidopsis. CycC1;1 physically interacts with MYC2 in the nucleus to inhibit MYC2-mediated transcriptional activation of senescence-associated genes (SAGs) by interfering with RNA polymerase II recruitment. Additionally, CycC1;1 interacts with the Mediator subunit MED25 to disrupt its association with MYC2. Disruption of CycC1;1 accelerates JA-dependent leaf yellowing, whereas loss of MYC2 or MED25 fully suppresses this premature-senescence phenotype. Unlike JAZ repressors, CycC1;1 expression and protein stability are uncoupled from JA signaling. Phylogenetic analyses suggest that the CycC1;1-MYC2 interaction may predate the emergence of JAZ repressors in aquatic ancestors, and CycC1;1 shows evolutionarily conserved ability to interact with and inhibit MYC2 across different plant species. Collectively, our findings uncover a CycC1;1-MED25-MYC2-regulatory module wherein CycC1;1 suppresses MYC2 activity by inhibiting MED25 binding to MYC2 and RNA polymerase II recruitment, downregulating SAG expression and thus delaying leaf senescence in plants. - Source: PubMed
Publication date: 2026/08/21
Liao Cai-YiHuang Xiao-LiLi LinLiu Guo-MaoLu Kai-KaiYang HongLi Song-QiJing Peng-WeiSong Ru-FengLiu Wen-Cheng - Direct chemical inhibition of transcription factor (TF)-cofactor interactions in plants remains challenging because their large protein-protein interfaces are poorly suited to conventional small molecules, while peptide-based inhibitors are limited by inefficient intracellular delivery. In our previous work, we demonstrated that peptide inhibitors can disrupt MYC transcription factor complexes in plants, but only at relatively high concentrations. Here, we show that a chemically defined chemocarrier overcomes this limitation and enables low-dose functional activity of peptide inhibitors in planta. To access TF-cofactor interfaces, we established a multi-step, target-guided screening platform that links in vitro high-throughput assays with functional validation in plants. This workflow integrates primary and secondary AlphaScreen assays using full-length and truncated MYC constructs with a tertiary assay targeting the interaction between MYCs and the MED25 coactivator. Screening of an approved-drug library followed by structure-activity optimization led to the identification of a low-toxicity aromatic derivative with potent cell-penetrating activity in Arabidopsis. Conjugation with this chemocarrier markedly enhanced the intracellular delivery and functional efficacy of multiple MYC-targeting peptide scaffolds, including cyclic and stapled peptides, resulting in over two orders of magnitude improvement in potency. This enabled robust inhibition of MYC-dependent transcriptional programs at substantially reduced concentrations, converting peptide-based inhibition from a high-dose proof-of-concept into a low-dose, functionally tractable strategy. These findings establish a practical chemical modality for accessing transcription factor-cofactor interfaces in plants. - Source: PubMed
Publication date: 2026/08/17
Liu RuiqiUehara YumaMino KoshikiIdei AkikoKimoto KazusaFujiwara DaisukeYoshida MinoruUeda MinoruTakaoka Yousuke - Plant specialized metabolites connect genetic programs and environmental responses with ecologically and economically valuable natural products. Their accumulation is rarely constitutive, varying instead with tissue identity, developmental stage, stress exposure, hormone signaling, and cellular storage capacity. This review examines basic helix-loop-helix (bHLH) transcription factors as regulatory switch points in plant specialized metabolism, with emphasis on the jasmonate-JAZ-MYC module. In resting tissues, JAZ repressors constrain MYC/bHLH activity; after wounding, herbivory, pathogen challenge, or elicitation, jasmonoyl-isoleucine triggers COI1-dependent JAZ turnover, releasing MYC factors to bind E-box/G-box motifs, recruit coregulators such as MED25, and activate biosynthetic genes or downstream transcription-factor cascades. Plant lineages have repeatedly adapted this regulatory logic to control terpenoids, alkaloids, phenylpropanoids, flavonoids, glucosinolates, phytoalexins, and related metabolites. Comparative examples include Arabidopsis sesquiterpenes and glucosinolates, Taxus taxanes, Artemisia artemisinin, Catharanthus terpenoid indole alkaloids, Salvia phenolic acids and tanshinones, Ginkgo terpene trilactones, rice diterpenoid phytoalexins, and cotton gossypol. Across these systems, bHLH output depends on dimer choice, promoter grammar, chromatin accessibility, hormone crosstalk, partner transcription factors, and cell-type competence. Six shared principles emerge: signal gating, topology matched to pathway architecture, partner-dependent promoter decoding, spatial competence, feedback rheostats, and evidence-dependent transferability. We further discuss evidence standards, multi-omics-guided factor discovery, miRNA-mediated post-transcriptional control, and engineering strategies for crop defense, food quality, medicinal-metabolite production, and synthetic biology. Unlike pathway- or MYC2-centered surveys, this review organizes the literature within a direct-cascade-hybrid framework that integrates promoter grammar, spatial competence, storage anatomy, and an explicit evidence hierarchy. - Source: PubMed
Publication date: 2026/08/03
Han XinpeiChen GuodongPeng JunCao NanLi FuguangWan Sumei - Numerous papillae structures form on the cell wall surface of Arabidopsis trichomes. Papillae do not develop in the Arabidopsis glassy hair3 (glh3) mutant. Cloning of the GLH3 gene revealed that a member of the pectate lyase gene family is required for papillae formation. GLH3 pectate lyase expression is trichome-specific in leaves and it precedes the appearance of papillae. The transcriptional Mediator complex containing Med25 and Med16 subunits activates GLH3 gene expression in trichomes. Following transport to the apoplast through a canonical secretion pathway, the GLH3-GFP fusion protein accumulates in papillae. Focused accumulation of the GLH3 pectate lyase in papillae suggests that papillae formation is driven by focal pectin hydrolysis. Trichome overexpression of another pectin metabolism gene, pectin methylesterase QRT1 prevented papillae formation. The presented data illustrate the role of spatially restricted pectin catabolism in altering cell surface topography by forming raised cell wall structures. - Source: PubMed
Publication date: 2026/08/05
Rickerd TrevorFornero ChristyDowell GabrielleAbdullah Abu Habib MdKirik Viktor - The Thr445Met substitution in the novel allele med25-5 uncouples seed dormancy from flowering, and MED25 acts as a negative regulator of seed dormancy via the DOG1 and ABA pathways. MED25, a pivotal subunit of the Mediator complex, regulates diverse biological processes, but its role in seed dormancy remains unclear. Here, we identified a novel MED25 allele, med25-5, harboring a Thr445Met substitution in the MD domain, which enhances seed dormancy without affecting flowering time in Arabidopsis thaliana. The med25-5 mutant exhibited increased dormancy with altered expressions in DOG1 and ABA signaling genes (e.g., ABI1, NHL6) and increased sensitivity to ABA and PAC. Either dog1-3 or abi3-10 can completely repress the enhanced seed dormancy of med25, indicating MED25 regulates dormancy requiring the DOG1 and ABA pathways. The Thr445 residue is conserved across crops, highlighting MED25's potential for crop improvement against pre-harvest sprouting. Our study uncovers MED25 as a negative regulator of seed dormancy, providing insights into the molecular mechanisms coordinating dormancy and flowering. - Source: PubMed
Publication date: 2026/07/02
Yang YueLi Xiao-YingDing RunCao HongLiu YongxiuLi Yu