SCARECROW (SCR) is a plant-specific GRAS-family nuclear transcriptional regulator that controls radial tissue patterning in Arabidopsis. Together with the mobile GRAS protein SHORT-ROOT (SHR), SCR forms a nuclear heterodimer that directs the asymmetric (formative) cell division of the cortex/endodermis initial and its daughter, generating the distinct cortex and endodermis cell layers, and specifies and maintains the root quiescent centre and the surrounding stem-cell niche. SCR sequesters SHR in the nucleus of the endodermal layer, restricting SHR intercellular movement to a single cell layer and reinforcing this through a SHR/SCR-dependent positive feedback loop on SCR transcription. The SHR-SCR heterodimer does not bind DNA directly; instead it acts as a transcriptional cofactor that recruits BIRD/INDETERMINATE DOMAIN (IDD) zinc-finger transcription factors such as JACKDAW (JKD), MAGPIE (MGP) and NUTCRACKER (NUC) to control ground-tissue target genes (including MGP, NUC and CYCLIN D6;1). SCR activity is spatially constrained by direct binding of the RETINOBLASTOMA-RELATED (RBR) protein through SCR's conserved LxCxE motif, forming a bistable circuit that confines asymmetric divisions to the stem-cell region. Beyond the root, SCR is expressed in the starch sheath of the hypocotyl and inflorescence stem, where its radial patterning function is required for shoot gravitropism, and in leaf bundle-sheath cells, where with SCR-LIKE 23 it specifies bundle-sheath fate. SCR also contributes to coordinating cell elongation, endodermal differentiation and redox homeostasis in the root.
Definition: A transcription coregulator activity in which a plant-specific GRAS-family protein, acting alone or as a GRAS-GRAS heterodimer, regulates target gene transcription by binding to a sequence-specific DNA-binding transcription factor (such as a BIRD/INDETERMINATE DOMAIN zinc-finger protein) rather than by binding DNA directly.
Justification: The SHR-SCR GRAS heterodimer regulates transcription via the DNA-binding BIRD/IDD factors and shows no evidence of direct DNA binding; a GRAS-specific cofactor term would more precisely capture this widely conserved mode of action than the generic coregulator term and avoid the inaccurate DNA-binding transcription factor activity annotations.
Parent term: transcription coregulator activity
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: SCR is a nuclear transcriptional regulator; nuclear localization is well established experimentally and by UniProt subcellular location. Reason: UniProt curates SCR as nuclear, and this is supported by multiple IDA observations (PMID:26494755, PMID:15314023) and by SCR sequestering SHR into the endodermal nucleus (PMID:17446396). The IEA subcellular-location mapping is correct. Supporting Evidence: PMID:17446396 SCARECROW (SCR) blocks SHR movement by sequestering it into the nucleus through protein-protein interaction |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000108 | ACCEPT | Summary: SCR is a transcriptional regulator that, in the SHR-SCR heterodimer, controls expression of ground-tissue target genes (MGP, NUC, CYCD6;1). Reason: This is the IBA/GO_Central-supported core biological process for SCR. The SHR-SCR complex regulates target gene transcription, even though it does so as a cofactor recruiting BIRD/IDD DNA-binding factors rather than by direct DNA binding (PMID:28211915). The term is at an appropriate level of generality. Supporting Evidence: PMID:28211915 These results suggest that SHR-SCR are transcriptional cofactors that regulate target gene transcription via binding of SHR to BIRD transcription factors. PMID:26494755 the BIRDs and SCARECROW regulate lineage identity, positional signals, patterning, and formative divisions throughout Arabidopsis root growth file:ARATH/SCR/SCR-deep-research-falcon.md SCR is a **putative transcriptional regulator/transcription factor** required for the asymmetric periclinal division that generates cortex and endodermis. |
| GO:0005515 protein binding | IPI PMID:17446396 An evolutionarily conserved mechanism delimiting SHR movemen... | MODIFY | Summary: This IPI records the SCR-SHR interaction (with SHR, UniProtKB:Q9SZF7), the central functional interaction of SCR. The bare 'protein binding' term is uninformative. Reason: Per curation guidance, GO:0005515 'protein binding' should be replaced by a more informative molecular function. The partner here is the GRAS-family transcriptional coregulator SHR (a GRAS regulator that does not itself bind DNA directly), with which SCR forms a nuclear heterodimer (PMID:17446396, PMID:28211915). The informative replacement is protein-domain-specific binding (GO:0019904), capturing the GRAS-GRAS heterodimerization interaction rather than the generic protein binding term. Proposed replacements: protein domain specific binding Supporting Evidence: PMID:17446396 SCARECROW (SCR) blocks SHR movement by sequestering it into the nucleus through protein-protein interaction file:ARATH/SCR/SCR-deep-research-falcon.md Reviews further emphasize SCR’s direct interaction with SHR and SCR’s role in confining SHR to nuclei |
| GO:0005515 protein binding | IPI PMID:17785527 Arabidopsis JACKDAW and MAGPIE zinc finger proteins delimit ... | MODIFY | Summary: IPI for SCR interactions in the JKD/MGP-SHR-SCR network (WITH SHR Q9SZF7 and MGP Q9ZWA6). Uninformative bare protein binding. Reason: The interactions captured here (SHR, and the BIRD/IDD zinc-finger TFs JKD/MGP that act with SHR-SCR) are with transcription factors. Replace generic protein binding with DNA-binding transcription factor binding (GO:0140297). JKD/MGP are zinc-finger DNA-binding TFs that operate in a SHR-dependent feed-forward loop with SCR. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:17785527 JACKDAW and MAGPIE genes, which encode members of a plant-specific family of zinc finger proteins, act in a SHR-dependent feed-forward loop to regulate the range of action of SHORT-ROOT and SCARECROW |
| GO:0005515 protein binding | IPI PMID:18500650 Large-scale analysis of the GRAS gene family in Arabidopsis ... | MODIFY | Summary: IPI recording the Y2H-confirmed SCR-SHR interaction from the GRAS-family survey (WITH SHR Q9SZF7). Reason: The interaction is with the GRAS-family coregulator SHR (a GRAS regulator that does not itself bind DNA directly), confirmed by yeast two-hybrid. Replace bare protein binding with protein-domain-specific binding (GO:0019904), capturing the GRAS-GRAS heterodimerization interaction. Proposed replacements: protein domain specific binding Supporting Evidence: PMID:18500650 we confirmed the protein-protein interaction between SHORT-ROOT (SHR) and SCARECROW (SCR) |
| GO:0005515 protein binding | IPI PMID:22921914 A bistable circuit involving SCARECROW-RETINOBLASTOMA integr... | MODIFY | Summary: IPI capturing the direct SCR-RBR (RETINOBLASTOMA-RELATED, UniProtKB:Q9LKZ3) interaction and SCR-SHR (Q9SZF7), via SCR's LxCxE motif. Reason: SCR binds the RBR pocket protein directly through its conserved LxCxE motif (residues 295-299), a functionally important interaction that spatially restricts asymmetric cell division. Bare protein binding is uninformative; this LxCxE-dependent RBR interaction is best captured by the more specific molecular function term protein-macromolecule adaptor / sequestering. As no clean verified term for 'pocket protein binding' is available in the existing set, propose DNA-binding transcription factor binding only partially fits; retain the essence but recommend replacement with a more informative term capturing the RBR interaction. Proposed replacements: protein domain specific binding Supporting Evidence: PMID:22921914 Spatial restriction of these divisions requires physical binding of the stem cell regulator SCARECROW (SCR) by the RETINOBLASTOMA-RELATED (RBR) protein. PMID:22921914 this interaction depends on the LxCxE motif in SCR. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | KEEP AS NON CORE | Summary: IPI from a large-scale binary interactome (phytohormone protein network) recording an SCR-GA2OX7 (UniProtKB:Q9C6I4) Y2H interaction. Reason: This is a single high-throughput binary interactome hit with a gibberellin 2-oxidase; its biological significance for SCR function is not established in the paper and it does not relate to SCR's characterised role. Bare protein binding is uninformative, but there is no specific partner-class function to substitute, and the interaction is peripheral. Retained as non-core pending validation. Supporting Evidence: PMID:32612234 a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0045454 cell redox homeostasis | IMP PMID:34056773 A mechanism coordinating root elongation, endodermal differe... | KEEP AS NON CORE | Summary: scr mutants accumulate elevated ROS in the root elongation zone, linked to reduced Peroxidase 3 expression; SCR coordinates elongation, endodermal differentiation and redox/oxidative-stress responses. Reason: This is a downstream physiological consequence of SCR's transcriptional role in endodermal differentiation rather than a core molecular function of SCR. The acts_upstream_of_or_within qualifier appropriately reflects an indirect relationship. Retain as a non-core process. Supporting Evidence: PMID:34056773 the scr mutant accumulated a higher level of reactive oxygen species (ROS) in the elongation zone, which is probably due to decreased expression of peroxidase gene 3 |
| GO:0005515 protein binding | IPI PMID:29352064 GIF Transcriptional Coregulators Control Root Meristem Homeo... | KEEP AS NON CORE | Summary: IPI linking SCR with AN3/GIF1 (AGI AT5G26840). In this study AN3/GIF coregulator complexes bind the SCR promoter; SCR is a transcriptional target of AN3 rather than a clearly established direct physical partner. Reason: The cited evidence shows AN3 complexes bind the SCR promoter region (regulatory relationship), not a well-defined SCR molecular-function interaction. Bare protein binding is uninformative and the relationship is peripheral to SCR's own function, so it is retained as non-core rather than used to define a core MF. Supporting Evidence: PMID:29352064 AN3 complexes bind directly to the promoter regions of PLT1 as well as SCARECROW |
| GO:0048364 root development | IGI PMID:26494755 Transcriptional control of tissue formation throughout root ... | ACCEPT | Summary: SCR, with the BIRDs and SHR, organizes tissue patterns and formative divisions throughout root growth, and is a postembryonic determinant of ground-tissue stem cells. Reason: Root development is a core biological process for SCR, supported by genetic interaction analysis with BIRD/IDD factors and SHR (PMID:26494755) and by the classic scr root phenotype (PMID:8756724). Appropriately broad parent term for the root patterning role. Supporting Evidence: PMID:26494755 the BIRDs and SCARECROW regulate lineage identity, positional signals, patterning, and formative divisions throughout Arabidopsis root growth file:ARATH/SCR/SCR-deep-research-falcon.md SCR’s best-supported primary function is controlling the formative division that creates cortex and endodermis, thereby establishing the root’s radial architecture |
| GO:0005634 nucleus | ISM GO_REF:0000122 | ACCEPT | Summary: Sequence-based (AtSubP) prediction of nuclear localization, consistent with experimental evidence. Reason: Nuclear localization of SCR is firmly established experimentally (IDA, PMID:26494755, PMID:15314023). The ISM prediction agrees with this. Supporting Evidence: PMID:26494755 These transcription factors are postembryonic determinants of the ground tissue stem cells and their lineage. |
| GO:0005515 protein binding | IPI PMID:28211915 Structure of the SHR-SCR heterodimer bound to the BIRD/IDD t... | MODIFY | Summary: IPI from the crystallographic study recording SCR interactions with JKD (UniProtKB:Q700D2) and SHR (UniProtKB:Q9SZF7). Bare protein binding is uninformative. Reason: This structural study defines SCR as part of the SHR-SCR heterodimer that, together, binds the BIRD/IDD zinc-finger DNA-binding transcription factor JKD. SCR binds the GRAS coregulator SHR directly (SHR is itself a GRAS regulator that does not bind DNA directly), and the SHR-SCR heterodimer in turn engages the DNA-binding transcription factor JKD; replace generic protein binding with DNA-binding transcription factor binding (GO:0140297), justified by the JKD partner. Note that JKD contacts SHR, not SCR, in the ternary complex. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:28211915 form a head-to-head 1:1 heterodimer PMID:28211915 These results suggest that SHR-SCR are transcriptional cofactors that regulate target gene transcription via binding of SHR to BIRD transcription factors. |
| GO:0005515 protein binding | IPI PMID:28746306 In vivo FRET-FLIM reveals cell-type-specific protein interac... | MODIFY | Summary: IPI from in vivo FRET-FLIM recording cell-type-specific SCR interactions (WITH AT4G37650/SHR and AT5G03150/JKD) and higher-order complexes. Reason: FRET-FLIM confirms SCR forms cell-type-specific complexes with the transcription factors SHR and JKD in vivo. The informative replacement for bare protein binding is DNA-binding transcription factor binding (GO:0140297), capturing the TF partner class. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:28746306 three fully functional fluorescently tagged cell fate regulators establish cell-type-specific interactions at endogenous expression levels and can form higher order complexes file:ARATH/SCR/SCR-deep-research-falcon.md coexpression of **JKD-YFP** with **SCR-RFP** reduced fluorescence lifetime by up to **0.17 ± 0.02 ns**, supporting close interaction/complex formation in meristem peripheral/primordia regions |
| GO:0003700 DNA-binding transcription factor activity | IMP PMID:26494755 Transcriptional control of tissue formation throughout root ... | MODIFY | Summary: SCR functions as a transcriptional regulator of ground-tissue genes, but structural/biochemical evidence indicates the SHR-SCR complex regulates transcription as a cofactor via BIRD/IDD DNA-binding partners, not by direct sequence-specific DNA binding. Reason: PMID:26494755 establishes SCR as a transcriptional regulator by mutant analysis, but it does not demonstrate direct sequence-specific DNA binding by SCR. The crystallographic and EMSA work (PMID:28211915) shows there is no evidence for direct DNA binding by SHR-SCR and that they act as transcription cofactors via BIRD/IDD factors. The annotation should be modified from DNA-binding transcription factor activity to a coregulator/cofactor molecular function. Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:28211915 there is no evidence for direct binding of SHR-SCR or other GRAS proteins to DNA PMID:28211915 These results suggest that SHR-SCR are transcriptional cofactors that regulate target gene transcription via binding of SHR to BIRD transcription factors. |
| GO:0005634 nucleus | IDA PMID:26494755 Transcriptional control of tissue formation throughout root ... | ACCEPT | Summary: Direct (IDA) evidence of SCR nuclear localization in root cells. Reason: SCR is a nuclear transcriptional regulator; direct observation of nuclear localization is consistent with all evidence and with the UniProt subcellular location. Core localization. Supporting Evidence: PMID:26494755 These transcription factors are postembryonic determinants of the ground tissue stem cells and their lineage. |
| GO:0008356 asymmetric cell division | IMP PMID:26494755 Transcriptional control of tissue formation throughout root ... | ACCEPT | Summary: SCR, with SHR and the BIRDs, acts as an effector of the asymmetric (formative) divisions that pattern the ground tissue into cortex and endodermis. Reason: Control of asymmetric cell division is a defining core function of SCR, supported here by genetic/transcriptomic analysis (PMID:26494755) and by the original cloning phenotype (PMID:8756724) and mosaic clonal analysis (PMID:15314023). Supporting Evidence: PMID:26494755 they direct asymmetric cell divisions and patterning of cell types PMID:15314023 SCR acts cell-autonomously to control asymmetric cell division within the ground tissue |
| GO:0090610 bundle sheath cell fate specification | IMP PMID:24517883 SCARECROW, SCR-LIKE 23 and SHORT-ROOT control bundle sheath ... | KEEP AS NON CORE | Summary: SCR (with SCL23 and SHR) specifies bundle-sheath cell fate in leaves; SCR is expressed in bundle-sheath cells and contributes to their sugar transport function. Reason: This is a genuine, experimentally supported role, but it is a tissue-specific developmental output in the leaf that is distinct from SCR's central root radial-patterning function. Retain as a non-core process for this pleiotropic regulator. Supporting Evidence: PMID:24517883 mutations in three GRAS family transcription factors, SHORT-ROOT (SHR), SCARECROW (SCR) and SCARECROW-LIKE 23 (SCL23), affect BS cell fate in Arabidopsis thaliana |
| GO:0048366 leaf development | IGI PMID:24517883 SCARECROW, SCR-LIKE 23 and SHORT-ROOT control bundle sheath ... | KEEP AS NON CORE | Summary: SCR contributes to leaf development through bundle-sheath cell fate specification, acting redundantly with SCL23 (AGI AT5G41920). Reason: Leaf development is a broad process reflecting SCR's bundle-sheath role; it is a peripheral, tissue-specific developmental output rather than a core function. Retain as non-core. Supporting Evidence: PMID:24517883 their expression pattern and function diverge at later stages of leaf development |
| GO:0042803 protein homodimerization activity | IPI NOT PMID:17446396 An evolutionarily conserved mechanism delimiting SHR movemen... | ACCEPT | Summary: NOT annotation - SCR does not homodimerize; it forms a heterodimer with SHR (the partner recorded is SHR, AGI AT3G54220 being SCR itself in the WITH field reflects the assay context). Reason: This correctly negated annotation captures that SCR does not self-associate into a functional homodimer; its functional unit is the SHR-SCR heterodimer (PMID:17446396, PMID:28211915). The negation is informative and consistent with the structural data showing a head-to-head SHR-SCR (not SCR-SCR) heterodimer. Supporting Evidence: PMID:28211915 form a head-to-head 1:1 heterodimer |
| GO:0051457 maintenance of protein location in nucleus | IMP PMID:17446396 An evolutionarily conserved mechanism delimiting SHR movemen... | ACCEPT | Summary: SCR sequesters the mobile SHR protein in the endodermal nucleus, restricting SHR intercellular movement to a single cell layer. Reason: A well-supported, specific functional role - SCR maintains SHR's nuclear location via direct protein-protein interaction, delimiting SHR movement and defining a single endodermal layer (PMID:17446396). This is a distinctive and core aspect of SCR function. Supporting Evidence: PMID:17446396 SCARECROW (SCR) blocks SHR movement by sequestering it into the nucleus through protein-protein interaction file:ARATH/SCR/SCR-deep-research-falcon.md restricting SHR to the nucleus and coordinating downstream patterning and stem cell niche functions |
| GO:0005634 nucleus | IDA PMID:15314023 Mosaic analyses using marked activation and deletion clones ... | ACCEPT | Summary: Direct evidence of nuclear SCR from mosaic clonal analysis of SCR action. Reason: Consistent with all evidence that SCR is a nuclear transcriptional regulator. Core localization. Supporting Evidence: PMID:15314023 SCR acts cell-autonomously to control asymmetric cell division within the ground tissue |
| GO:0043565 sequence-specific DNA binding | IDA PMID:17446396 An evolutionarily conserved mechanism delimiting SHR movemen... | REMOVE | Summary: Annotation of direct sequence-specific DNA binding by SCR. Subsequent structural and biochemical analysis directly refutes direct DNA binding by GRAS proteins including SHR-SCR. Reason: The crystal structures of the SHR-SCR and JKD-SHR-SCR complexes found no DNA-binding motif, an overall negatively charged surface unfavorable for DNA binding, and no detectable direct DNA binding by SHR-SCR; the complex regulates transcription indirectly through BIRD/IDD zinc-finger factors (PMID:28211915). SCR/SHR do associate with target promoters (e.g. NUC, MGP), but the evidence indicates this is via DNA-binding partner proteins rather than intrinsic sequence-specific DNA binding by SCR. Because the structural evidence actively contradicts (rather than merely broadens) a direct sequence-specific DNA-binding activity, the IDA annotation is incorrect and should be removed. Supporting Evidence: PMID:28211915 there is no evidence for direct binding of SHR-SCR or other GRAS proteins to DNA PMID:28211915 We did not find any DNA-binding motifs in our structure of the SHR-SCR complex |
| GO:0009956 radial pattern formation | IMP PMID:10631180 Molecular analysis of SCARECROW function reveals a radial pa... | ACCEPT | Summary: SCR controls radial patterning of ground tissue in both root and shoot; scr mutants lose a ground-tissue layer (root) and the starch sheath (hypocotyl/stem). Reason: Radial pattern formation is a core biological process for SCR, demonstrated by the scr radial-patterning defects in root and shoot and the correlation between defective divisions and SCR expression (PMID:10631180). Well supported and central. Supporting Evidence: PMID:10631180 both hypocotyl and shoot inflorescence also have a radial pattern defect, loss of a normal starch sheath layer file:ARATH/SCR/SCR-deep-research-falcon.md generating separate **cortex** and **endodermis** layers and thus normal **radial organization** |
| GO:0003700 DNA-binding transcription factor activity | ISS PMID:11118137 Arabidopsis transcription factors: genome-wide comparative a... | MODIFY | Summary: Sequence/family-based classification of SCR as a GRAS-family putative transcription factor in a genome-wide TF survey. Reason: This ISS reflects classification of GRAS proteins as putative transcription factors based on sequence/family membership. However, direct DNA-binding transcription factor activity has not been demonstrated for SCR; structural and biochemical data indicate SHR-SCR act as transcription cofactors via BIRD/IDD DNA-binding partners (PMID:28211915). Modify to the more accurate coregulator/cofactor molecular function. Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:11118137 Arabidopsis dedicates over 5% of its genome to code for more than 1500 transcription factors, about 45% of which are from families specific to plants. PMID:28211915 These results suggest that SHR-SCR are transcriptional cofactors that regulate target gene transcription via binding of SHR to BIRD transcription factors. |
| GO:0008356 asymmetric cell division | IMP PMID:8756724 The SCARECROW gene regulates an asymmetric cell division tha... | ACCEPT | Summary: The founding study - scr disrupts the asymmetric division that generates cortex and endodermis, leaving a single mixed-identity ground-tissue layer. Reason: This is the defining core function of SCR, established by the original mutant phenotype (PMID:8756724). The asymmetric cell division of the cortex/endodermis initial and its daughter is the central process SCR controls. Supporting Evidence: PMID:8756724 The scarecrow mutation results in roots that are missing one cell layer owing to the disruption of an asymmetric division that normally generates cortex and endodermis. file:ARATH/SCR/SCR-deep-research-falcon.md In **scr** mutants, the second asymmetric division fails and a **single heterogeneous ground-tissue layer** forms instead of separate cortex and endodermis |
| GO:0009630 gravitropism | IMP PMID:10322541 The endodermis and shoot gravitropism. | KEEP AS NON CORE | Summary: SCR (=SGR1) is required for shoot gravitropism because the endodermis/starch sheath, whose formation depends on SCR, is the site of gravity perception in shoots. Reason: The gravitropism defect is an indirect physiological consequence of SCR's radial-patterning role in forming the starch sheath, rather than a distinct core function. The acts_upstream_of_or_within qualifier is appropriate. Retain as a non-core process. Supporting Evidence: PMID:10322541 shoot gravitropism 1 (sgrl), which is allelic to scarecrow (scr) ... indicate that the endodermis is the site of gravity perception in shoots file:ARATH/SCR/SCR-deep-research-falcon.md amyloplasts in scr do not sediment in response to gravity |
| GO:0003700 DNA-binding transcription factor activity | ISS PMID:8756724 The SCARECROW gene regulates an asymmetric cell division tha... | MODIFY | Summary: Inference from the original cloning that SCR is a member of a novel family of putative transcription factors (later defined as GRAS). Reason: The original sequence-based inference correctly identified SCR as a putative transcription factor, but direct DNA-binding TF activity has not been shown. Current structural/biochemical evidence shows SHR-SCR act as transcription cofactors via BIRD/IDD DNA-binding partners (PMID:28211915). Modify to transcription coregulator activity for accuracy. Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:8756724 The deduced amino acid sequence of SCARECROW (SCR) suggests that it is a member of a novel family of putative transcription factors. PMID:28211915 there is no evidence for direct binding of SHR-SCR or other GRAS proteins to DNA |
Loading supporting content…
Download this section (compressed HTML)Q: Does SCR contact target-gene promoters only indirectly through BIRD/IDD partners, or does SCR/SHR make any direct DNA contacts in vivo (e.g. by ChIP combined with partner-protein depletion)?
Q: What is the molecular role of SCR (versus SHR) within the SHR-SCR-BIRD ternary complex, given that JKD contacts SHR but not SCR in the crystal structure?
Experiment: Genome-wide ChIP-seq for SCR and SHR with and without JKD/MGP/NUC function to test whether SCR promoter occupancy depends on BIRD/IDD DNA-binding partners.
Experiment: In vitro EMSA/SELEX with purified SCR and SHR-SCR to formally test for any intrinsic sequence-specific DNA-binding activity.
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)