SEPALLATA3 (SEP3/AGL9; At1g24260) encodes a nuclear MIKC-type MADS-box transcription factor that acts as an E-class floral homeotic regulator in Arabidopsis thaliana. SEP3 binds CArG-box cis-regulatory DNA through its MADS domain and uses its K-box/coiled-coil region to form homo- and heteromeric MADS transcription-factor complexes. In floral tissues, these complexes cooperate with AP1, AP3/PI, AG, SHP/STK/TT16-class MADS proteins and transcription/chromatin coregulators to regulate RNA-polymerase-II target genes controlling floral organ identity, floral organ morphogenesis, ovule development and floral meristem determinacy. The strongest core evidence supports SEP3 as a chromatin-associated transcription factor and interaction hub for floral quartet-like complexes; seed coat and mucilage phenotypes are reported but require full-text review before being treated as curated SEP3 functions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001708 cell fate specification | IMP PMID:10821278 B and C floral organ identity functions require SEPALLATA MA... | MODIFY | Summary: The sep1 sep2 sep3 mutant phenotype supports a role in specifying floral organ fates, but the parent term cell fate specification is too broad for the available evidence. Reason: The source evidence concerns floral organ identity, specifically loss of petals, stamens and carpels in SEP1/2/3-deficient flowers. A floral-organ-specific replacement captures the same biology without generalizing to cell fate specification outside flower development. Proposed replacements: specification of floral organ identity Supporting Evidence: PMID:10821278 Triple mutant Arabidopsis plants lacking the activity of all three SEP genes produce flowers in which all organs develop as sepals. |
| GO:0009908 flower development | TAS PMID:11439126 APETALA1 and SEPALLATA3 interact to promote flower developme... | ACCEPT | Summary: SEP3 promotes flower development through interaction with AP1 and through its broader E-class role in floral homeotic transcription-factor complexes. Reason: Although broad, flower development is an appropriate high-level biological process for SEP3. The source abstract directly reports SEP3 interaction with AP1 and flower-development phenotypes, and multiple additional sources support this as part of SEP3's core developmental program. Supporting Evidence: PMID:11439126 Taken together, these studies suggest that SEP3 interacts with AP1 to promote normal flower development. |
| GO:0010093 specification of floral organ identity | IMP PMID:10821278 B and C floral organ identity functions require SEPALLATA MA... | ACCEPT | Summary: The sep1 sep2 sep3 triple mutant converts petals, stamens and carpels to sepaloid organs, directly supporting SEP-family involvement in floral organ identity specification. Reason: Floral organ identity specification is the best biological-process term for the genetic phenotype reported in the source. SEP3 acts redundantly with SEP1 and SEP2, but the annotation correctly captures the process in which SEP3 participates. Supporting Evidence: PMID:10821278 SEP1/2/3 are a class of organ-identity genes that is required for development of petals, stamens and carpels. |
| GO:0010093 specification of floral organ identity | IMP PMID:19385720 Target genes of the MADS transcription factor SEPALLATA3: in... | ACCEPT | Summary: Genome-wide SEP3 binding and dominant-repressor phenotypes support SEP3 as a direct transcriptional regulator in the floral organ identity network. Reason: The paper directly studies SEP3 target binding and the developmental consequences of blocking SEP3-mediated activation. This supports retaining the floral organ identity specification annotation. Supporting Evidence: PMID:19385720 SEP3 is a member of the SEP subfamily of MADS-box genes, whose members have nearly redundant functions in the specification of floral meristem identity and in the identity of all types of floral organs |
| GO:0010214 seed coat development | IMP PMID:32519347 Identification of novel seed longevity genes related to oxid... | KEEP AS NON CORE | Summary: A reverse-genetic seed longevity screen links the sep3 knockout to a seed-coat-related seed ageing phenotype. This is a non-core role. Reason: The source full text is unavailable locally, but the abstract reports a reverse-genetic sep3 knockout phenotype and places SEP3 among the genes that support the protective role of the seed coat. The curator read the full text and assigned an acts_upstream_of_or_within IMP annotation, and that qualifier already allows an indirect role. The term is kept as a non-core, possibly indirect, late reproductive phenotype. It is not part of SEP3's core floral organ identity function. Supporting Evidence: PMID:32519347 The cytochrome P-450 hydroxylase, CYP86A8, and the transcription factors, MYB47, KNAT7 and SEP3, support the protecting role of the seed coat during seed ageing. |
| GO:0048481 plant ovule development | IMP PMID:14555696 MADS-box protein complexes control carpel and ovule developm... | KEEP AS NON CORE | Summary: SEP proteins participate in multimeric MADS complexes required for normal ovule development, but this is a later reproductive-organ role rather than the primary gene-level function. Reason: The full text provides genetic and interaction evidence that reduced SEP activity disrupts ovule development. However, the evidence is SEP-family-redundant and process-level; SEP3's core function is the DNA-binding and complex-forming transcription-factor activity that contributes to this process. Supporting Evidence: PMID:14555696 a reduction in SEP activity leads to the loss of normal ovule development |
| GO:0048833 specification of floral organ number | IMP PMID:19385720 Target genes of the MADS transcription factor SEPALLATA3: in... | MARK AS OVER ANNOTATED | Summary: Dominant repression of SEP3 target genes causes reduced numbers and sizes of floral organs, but the term overstates a direct SEP3 role in specifying organ number. Reason: The source supports SEP3 as a transcriptional regulator of floral organ morphogenesis and growth-related target genes. The floral organ number phenotype appears to be a consequence of disrupting SEP3-regulated programs rather than a distinct core process that SEP3 specifically specifies. Supporting Evidence: PMID:19385720 transgenic lines with a strong phenotype showed delayed flowering (unpublished data), reduced number and size of floral organs, as well as defects in organ differentiation |
| GO:0080001 mucilage extrusion from seed coat | IMP PMID:32519347 Identification of novel seed longevity genes related to oxid... | KEEP AS NON CORE | Summary: A seed-coat phenotype of the sep3 knockout, recorded by the GOA curator from the full text of a reverse-genetic seed longevity study. It is a non-core, possibly indirect, late reproductive role. Reason: The full text is not in PMC or Europe PMC (no PMCID) and could not be read, so the specific mucilage data were not seen. The abstract shows that the study phenotyped seed-coat properties of the knockout mutants and placed SEP3 among the genes that support the protective role of the seed coat. A mucilage extrusion phenotype is therefore plausible. Per project policy, I defer to the curator, who read the full text, rather than overrule an experimental annotation. The acts_upstream_of_or_within qualifier already allows an indirect role. This term is not part of SEP3's core floral organ identity function. Supporting Evidence: PMID:32519347 support the protecting role of the seed coat during seed ageing. |
| GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro domain evidence and experimental SEP3 studies support sequence-specific binding to transcriptional regulatory DNA. Reason: SEP3 is a MADS-box transcription factor that binds CArG-box regulatory DNA. This electronically inferred term is consistent with both the domain architecture and direct DNA-binding studies. Supporting Evidence: file:ARATH/SEP3/SEP3-uniprot.txt DR InterPro; IPR033896; MEF2-like_N. PMID:19033361 bind cooperatively to two sequence elements termed 'CArG boxes' |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: The PANTHER/IBA inference is appropriate for SEP3, a conserved MADS-box/MEF2 transcription factor with experimentally demonstrated CArG-box cis-regulatory DNA binding. Reason: The term captures the core DNA-binding activity more precisely than generic DNA binding. SEP3 is in the PTHR48019 MADS-box/MEF2 family and has direct biochemical and ChIP evidence for binding regulatory DNA. Supporting Evidence: file:interpro/panther/PTHR48019/PTHR48019-entries.csv O22456,Developmental protein SEPALLATA 3,protein,3702,Arabidopsis thaliana,Arabidopsis thaliana (Mouse-ear cress),SEP3,251 PMID:19385720 SEPALLATA3 binds to thousands of sites in the genome. |
| GO:0003677 DNA binding | IEA GO_REF:0000002 | MODIFY | Summary: SEP3 is DNA-binding, but the generic parent term loses the transcriptional cis-regulatory specificity supported by MADS-box domain evidence. Reason: InterPro domain mappings support a MADS-box DNA-binding protein, but SEP3 should be annotated to the more informative RNA-polymerase-II cis-regulatory region sequence-specific DNA-binding term. Proposed replacements: RNA polymerase II cis-regulatory region sequence-specific DNA binding Supporting Evidence: file:ARATH/SEP3/SEP3-uniprot.txt FT DOMAIN 3..57 |
| GO:0003677 DNA binding | IDA PMID:19033361 The class E floral homeotic protein SEPALLATA3 is sufficient... | MODIFY | Summary: The direct assay shows SEP3 binding to CArG-box DNA and cooperative looping, so the generic DNA binding term should be replaced by the regulatory-region-specific binding term. Reason: The experimental evidence is not merely generic DNA binding; it tests SEP3 binding to CArG-box cis-regulatory sequences as a floral homeotic transcription factor. Proposed replacements: RNA polymerase II cis-regulatory region sequence-specific DNA binding Supporting Evidence: PMID:19033361 homotetramers of the class E floral homeotic protein SEPALLATA3 from Arabidopsis thaliana bind cooperatively to two sequence elements termed 'CArG boxes' |
| GO:0003700 DNA-binding transcription factor activity | IEA GO_REF:0000002 | MODIFY | Summary: The annotation is directionally correct but should use the current RNA-polymerase-II-specific DNA-binding transcription factor activity term. Reason: SEP3 regulates transcription of nuclear protein-coding target genes and belongs to the MADS-box/MEF2 transcription-factor family. GO:0000981 is a more specific and current replacement for this generic transcription factor activity. Proposed replacements: DNA-binding transcription factor activity, RNA polymerase II-specific Supporting Evidence: file:interpro/panther/PTHR48019/PTHR48019-metadata.yaml The MADS-box/MEF2 family proteins are transcription factors |
| GO:0003700 DNA-binding transcription factor activity | ISS PMID:11118137 Arabidopsis transcription factors: genome-wide comparative a... | MODIFY | Summary: The original sequence-similarity source supports Arabidopsis transcription-factor family membership, but the GO term should be updated to the RNA-polymerase-II-specific activity. Reason: Family-level evidence and SEP3-specific experiments support a DNA-binding transcription factor role. The replacement term better represents SEP3 as a protein-coding gene transcription regulator. Proposed replacements: DNA-binding transcription factor activity, RNA polymerase II-specific Supporting Evidence: PMID:11118137 Arabidopsis dedicates over 5% of its genome to code for more than 1500 transcription factors |
| GO:0003700 DNA-binding transcription factor activity | TAS PMID:11439126 APETALA1 and SEPALLATA3 interact to promote flower developme... | MODIFY | Summary: SEP3 is a MADS-box DNA-binding transcription factor, but the annotation should be modernized to GO:0000981. Reason: The publication supports SEP3's role in floral transcription-factor complexes with AP1. The current best MF term is RNA-polymerase-II-specific DNA-binding transcription factor activity. Proposed replacements: DNA-binding transcription factor activity, RNA polymerase II-specific Supporting Evidence: PMID:11439126 SEP3 interacts with AP1 to promote normal flower development. |
| GO:0003700 DNA-binding transcription factor activity | ISS PMID:12837945 Molecular and phylogenetic analyses of the complete MADS-box... | MODIFY | Summary: MADS-box family evidence supports SEP3 as a transcription factor, but the term should be replaced with the RNA-polymerase-II-specific child term. Reason: The original source is a family analysis, and stronger SEP3-specific evidence supports using GO:0000981 rather than the generic GO:0003700 term. Proposed replacements: DNA-binding transcription factor activity, RNA polymerase II-specific Supporting Evidence: PMID:12837945 MADS-box transcription factors are key regulators of several plant development processes. |
| GO:0005515 protein binding | IPI PMID:14555696 MADS-box protein complexes control carpel and ovule developm... | MODIFY | Summary: The underlying evidence concerns SEP-dependent multimeric MADS complexes with AG/SHP/STK-class proteins during carpel and ovule development. Reason: Generic protein binding should not be retained. The evidence supports MADS protein heteromerization as the informative molecular activity. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:14555696 STK, AG, SHP1, and SHP2 can form multimeric complexes and that these interactions require the SEPALLATA (SEP) MADS-box proteins. |
| GO:0005515 protein binding | IPI PMID:15604664 Defining subdomains of the K domain important for protein-pr... | MODIFY | Summary: The annotation reflects K-domain-mediated heteromeric interactions between SEP3 and B-class MADS proteins, not nonspecific protein binding. Reason: The more informative term is protein heterodimerization activity, because the study maps domains required for PI/SEP3 interactions. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:15604664 The strong PI/SEP3 (or PI/SEP1) interaction requires K2 |
| GO:0005515 protein binding | IPI PMID:15805477 Comprehensive interaction map of the Arabidopsis MADS Box tr... | MODIFY | Summary: The publication reports a broad MADS-box transcription-factor interaction map, including SEP3 partners in floral regulatory complexes. Reason: The generic protein binding term should be replaced by protein heterodimerization activity for SEP3 interactions with other MADS transcription factors. Full text is not locally available, so partner specificity is taken from the GOA/IntAct lines and the abstract-level interaction-map evidence. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:15805477 revealed a collection of specific heterodimers and a few homodimers. |
| GO:0005515 protein binding | IPI PMID:16080001 Mutant analysis, protein-protein interactions and subcellula... | MODIFY | Summary: This evidence specifically supports heterodimerization of SEP3 with the B-sister MADS protein ABS/TT16. Reason: Heterodimerization is the informative molecular function. Generic protein binding should not be retained for a well-characterized MADS-MADS interaction. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:16080001 Heterodimerization of ABS with SEP3 was confirmed by gel retardation assays. |
| GO:0005515 protein binding | IPI PMID:16854969 APETALA1 and SEPALLATA3 interact with SEUSS to mediate trans... | MODIFY | Summary: SEP3 binds the transcriptional corepressor SEUSS, linking a DNA-binding MADS protein to SEU/LUG-mediated transcriptional repression. Reason: The specific functional interaction is transcription coregulator binding, not generic protein binding. Proposed replacements: transcription coregulator binding Supporting Evidence: PMID:16854969 APETALA1 (AP1) and SEPALLATA3 (SEP3), both MADS box DNA-binding proteins, interacted with SEU. |
| GO:0005515 protein binding | IPI PMID:16925602 A Bsister MADS-box gene involved in ovule and seed developme... | MODIFY | Summary: The B-sister study supports formation of higher-order MADS complexes that include E-class SEP proteins, including SEP3-related interaction evidence. Reason: Protein heterodimerization activity is a more informative molecular function than generic protein binding for MADS transcription-factor complex formation. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:16925602 Protein interaction studies revealed the formation of higher-order complexes between B(s)-C-E and B(s)-D-E type MADS-box proteins |
| GO:0005515 protein binding | IPI PMID:22323601 SWI2/SNF2 chromatin remodeling ATPases overcome polycomb rep... | MODIFY | Summary: SEP3 physically interacts with the SWI/SNF chromatin-remodeling ATPases SYD and BRM during activation of floral homeotic genes. Reason: The specific interaction is with transcription/chromatin coregulators recruited to floral homeotic loci, so transcription coregulator binding is more informative than generic protein binding. Proposed replacements: transcription coregulator binding Supporting Evidence: PMID:22323601 physically interact with two direct transcriptional activators of class B and class C gene expression, LEAFY (LFY) and SEPALLATA3 (SEP3). |
| GO:0005515 protein binding | IPI PMID:24714165 Phytoplasma effector SAP54 hijacks plant reproduction by deg... | REMOVE | Summary: SAP54 binding to SEP3 is a phytoplasma effector-host interaction that causes pathogen-mediated degradation of floral MADS transcription factors. Reason: This interaction is biologically real but represents pathogen targeting of SEP3 rather than an endogenous SEP3 molecular function. It should not be retained as generic protein binding in a core GO annotation set. Supporting Evidence: PMID:24714165 SEPALLATA3 (SEP3) as SAP54 interactors |
| GO:0005515 protein binding | IPI PMID:36088536 The protein-protein interaction landscape of transcription f... | MODIFY | Summary: The GOA lines for this source list MADS transcription-factor partners for SEP3 during gynoecium-development interaction mapping, but the cached publication has only an abstract. Reason: The broad abstract and GOA partner list are consistent with transcription-factor heterodimerization, which is more informative than generic protein binding. Exact interaction details should be revisited if the full text becomes available. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:36088536 We analyzed almost 4500 combinations and detected more than 250 protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:37965720 Protein interaction mapping reveals widespread targeting of ... | REMOVE | Summary: This annotation reflects targeting of SEP3 by a phytoplasma effector protein rather than an endogenous SEP3 function. Reason: As with the earlier SAP54 study, phytoplasma effector binding should not be retained as generic protein binding for SEP3's normal molecular function. The full text is not locally available, but the abstract supports the pathogen-effector context. Supporting Evidence: PMID:37965720 widespread, but specific, interactions between phytoplasma effectors and host transcription factors |
| GO:0046983 protein dimerization activity | IEA GO_REF:0000002 | MODIFY | Summary: SEP3 dimerizes and forms higher-order MADS complexes, but the generic dimerization term should be split into more informative homo- and heterodimerization activities. Reason: UniProt and experimental studies support both SEP3 homomerization and heteromerization with other floral MADS proteins. Using the specific replacement terms improves functional precision. Proposed replacements: protein homodimerization activity protein heterodimerization activity Supporting Evidence: file:ARATH/SEP3/SEP3-uniprot.txt SUBUNIT: Forms homodimers PMID:19033361 homotetramers of the class E floral homeotic protein SEPALLATA3 |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000002 | MODIFY | Summary: SEP3 regulates transcription, but the term should be narrowed to RNA-polymerase-II transcription regulation. Reason: SEP3 is a nuclear DNA-binding transcription factor regulating protein-coding floral targets. GO:0006357 is the better general process term and is also present in the phylogenetic GOA set. Proposed replacements: regulation of transcription by RNA polymerase II Supporting Evidence: PMID:19385720 SEP3 acts mostly as a transcriptional activator |
| GO:0006357 regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference of RNA-polymerase-II transcription regulation is consistent with SEP3's conserved MADS-box transcription-factor function. Reason: This BP term accurately captures the process directly mediated by SEP3's DNA-binding transcription-factor and complex-forming activities. Supporting Evidence: PMID:19385720 the binding of the SEPALLATA3 protein to cis-regulatory elements of other MADS-box genes and expression analyses reveal that this protein is a key component in the regulatory transcriptional network underlying the formation of floral organs. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IEA GO_REF:0000002 | ACCEPT | Summary: SEP3 has strong evidence for transcriptional activation of floral homeotic programs, although it can also participate in repression depending on cofactors. Reason: The positive-regulation term is supported by SEP3 target-gene and chromatin-remodeler recruitment studies. It should be retained while also recognizing that SEP3 may bind co-repressors in some complexes. Supporting Evidence: PMID:22323601 required for formation of the male and female reproductive structures of the flower and for induction of AP3 and AG expression. |
| GO:0005634 nucleus | IEA GO_REF:0000002 | ACCEPT | Summary: Nuclear localization is consistent with SEP3's MADS-box transcription factor domains and chromatin-bound regulatory activity. Reason: SEP3 functions at nuclear cis-regulatory DNA. Multiple independent sources support a nuclear location. Supporting Evidence: file:ARATH/SEP3/SEP3-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping to nucleus is appropriate for SEP3. Reason: The UniProt record explicitly maps SEP3 to the nucleus and this is coherent with its transcription-factor function. Supporting Evidence: file:ARATH/SEP3/SEP3-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000117 | ACCEPT | Summary: The ARBA nuclear prediction is consistent with the curated evidence for a nuclear MADS-box transcription factor. Reason: Although computational, the annotation agrees with UniProt, direct functional evidence and experimental localization/complex assays. Supporting Evidence: file:ARATH/SEP3/SEP3-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | ISM GO_REF:0000122 | ACCEPT | Summary: AtSubP prediction of nuclear localization is consistent with SEP3's established cellular site of action. Reason: The prediction agrees with direct functional evidence that SEP3 binds chromatin and regulates transcription in the nucleus. Supporting Evidence: file:ARATH/SEP3/SEP3-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | HDA PMID:14617066 Analysis of the Arabidopsis nuclear proteome and its respons... | ACCEPT | Summary: The high-throughput Arabidopsis nuclear proteome annotation is consistent with SEP3's transcription-factor function, but the cached abstract does not identify SEP3 specifically. Reason: This HDA annotation is retained because it is supported by convergent direct and curated evidence for SEP3 acting in the nucleus. The original source itself is abstract-only locally, so the exact proteomics spot assignment was not rechecked. Supporting Evidence: PMID:14617066 In this study, we comprehensively characterized the Arabidopsis nuclear proteome. file:ARATH/SEP3/SEP3-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | IDA PMID:22238427 Characterization of MADS-domain transcription factor complex... | ACCEPT | Summary: In situ bimolecular fluorescence and floral MADS-complex experiments support SEP3-containing complexes acting in the nucleus during flower development. Reason: The source provides experimental evidence for MADS-domain protein interactions during meristematic stages and is consistent with nuclear localization of SEP3 regulatory complexes. Supporting Evidence: PMID:22238427 In situ bimolecular fluorescent complementation assays demonstrate that MADS-domain proteins interact during meristematic stages of flower development. |
| GO:0010582 floral meristem determinacy | IMP PMID:29562355 Tetramerization of MADS family transcription factors SEPALLA... | NEW | Summary: SEP3 contributes to floral meristem determinacy through tetramerization-dependent SEP3-AG complexes that activate determinacy targets such as KNU and CRC. Reason: This high-confidence SEP3 function is not represented in the seeded GOA annotations. The primary experimental work shows that tetramerization-defective SEP3 largely restores organ identity but fails to restore meristem determinacy, indicating that SEP3-containing tetrameric complexes are required for this process. Supporting Evidence: PMID:29562355 In contrast, while the carpel development program was launched, gynoecium development is incomplete due to a lack of determinacy of the floral meristem. |
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Download this section (compressed HTML)Q: Is SEP3 required directly for seed coat development and mucilage extrusion, or are the reported seed phenotypes indirect consequences of altered reproductive development or seed ageing?
Suggested experts: J. Renard, R. Niñoles
Q: Which endogenous SEP3-containing complexes act at ovule and seed-coat loci, and how do their target genes differ from the floral organ identity and meristem determinacy targets?
Suggested experts: G. C. Angenent, M. M. Kater
Q: Does isoform O22456-2, which lacks residue 90, measurably alter SEP3 dimerization, tetramerization or target-gene selection in vivo?
Suggested experts: C. Zubieta, F. Parcy
Experiment: In matched sep3 and higher-order sep backgrounds complemented with native-promoter SEP3, quantify seed coat morphology, mucilage extrusion and seed longevity, then compare with floral phenotype severity to separate direct seed-coat effects from pleiotropic reproductive defects.
Hypothesis: SEP3 has a direct, genetically separable role in seed coat development or mucilage extrusion.
Type: seed coat phenotyping and complementation
Experiment: Profile SEP3 occupancy in staged floral meristems, ovules and seed coats using native-tagged SEP3, then integrate RNA-seq from sep3/SEP-reduced tissues to identify direct targets for organ identity, ovule and seed-coat programs.
Hypothesis: SEP3 binds distinct cis-regulatory targets in ovules and developing seed coats compared with floral organ primordia.
Type: staged ChIP-seq or CUT&Tag
Experiment: Express isoform 1 and isoform 2 from comparable native SEP3 regulatory contexts in a sep3 sensitized background, then assay floral organ identity, determinacy, protein interactions and target-gene occupancy.
Hypothesis: SEP3 isoform 2 retains core MADS transcription-factor activity but may alter K-domain-dependent complex formation or target selection.
Type: isoform rescue assay
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