The PFYRE Subdomain in Master Growth Repressor DELLA is Essential for Its Association with Target Chromatin via Histone H2A Binding
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ABSTRACT:
PROVIDER: PRJNA911818 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR22715786_1.fastq.gz | Fastqsanger.gz | |||
| SRR22715786_2.fastq.gz | Fastqsanger.gz | |||
| SRR22715787_1.fastq.gz | Fastqsanger.gz | |||
| SRR22715787_2.fastq.gz | Fastqsanger.gz | |||
| SRR22715788_1.fastq.gz | Fastqsanger.gz |
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Project description:The DELLA genes encode conserved master growth repressors in plants, and they are also known as ‘Green Revolution’ genes because of their pivotal role in modulating stature of the high-yielding wheat varieties, which were crucial for the success of the ‘Green Revolution’ in the 1960s. At the cellular level, DELLA proteins are nuclear-localized transcription regulators, which play a central role in controlling plant development in response to internal and environmental cues. Recent studies indicate that DELLAs regulate expression of target genes via direct protein-protein interaction of their C-terminal GRAS domain with hundreds of key transcription factors (TFs) and epigenetic regulators. However, the molecular mechanism of DELLA-mediated transcription reprogramming remains unclear. Here, by characterizing missense alleles of an Arabidopsis DELLA, REPRESSOR OF ga1-3 (RGA), we unveil a novel function of the PFYRE subdomain within its GRAS domain for binding to histone H2A via pulldown and co-IP assays. ChIP-Seq analysis further show that this activity is essential for RGA association with its target chromatin globally. Our results indicate that although DELLAs are recruited to target gene promoters by binding to TFs via its LHR1 subdomain, DELLA-H2A interaction via its PFYRE subdomain is necessary to stabilize the TF-DELLA-H2A complex at the target chromatin. This study provides new insight into the two distinct key modular functions in DELLA for its genome-wide transcription regulation in plants. Chromatin immunoprecipitation DNA-sequencing (ChIP-seq) for RGA, rga-11 as well as the negative control sly1 dP and sly1 dQ.
2023-06-27 | GSE220898 | GEO
Project description:The DELLA genes encode conserved master growth repressors in plants, and they are also known as ‘Green Revolution’ genes because of their pivotal role in modulating stature of the high-yielding wheat varieties, which were crucial for the success of the ‘Green Revolution’ in the 1960s. At the cellular level, DELLA proteins are nuclear-localized transcription regulators, which play a central role in controlling plant development in response to internal and environmental cues. Recent studies indicate that DELLAs regulate expression of target genes via direct protein-protein interaction of their C-terminal GRAS domain with hundreds of key transcription factors (TFs) and epigenetic regulators. However, the molecular mechanism of DELLA-mediated transcription reprogramming remains unclear. Here, by characterizing missense alleles of an Arabidopsis DELLA, REPRESSOR OF ga1-3 (RGA), we unveil a novel function of the PFYRE subdomain within its GRAS domain for binding to histone H2A via pulldown and co-IP assays. ChIP-Seq analysis further show that this activity is essential for RGA association with its target chromatin globally. Our results indicate that although DELLAs are recruited to target gene promoters by binding to TFs via its LHR1 subdomain, DELLA-H2A interaction via its PFYRE subdomain is necessary to stabilize the TF-DELLA-H2A complex at the target chromatin. This study provides new insight into the two distinct key modular functions in DELLA for its genome-wide transcription regulation in plants. The assay for transposase-accessible chromatin using sequencing (ATAC-seq) for RGA vs rga-11 and RGA treated with GA or mock.
2023-06-27 | GSE233124 | GEO
Project description:DELLA proteins are conserved master growth regulators that play a central role in controlling plant development in response to internal and environmental cues. DELLAs function as transcription regulators, which are recruited to target promoters by binding to transcription factors (TFs) and histone H2A via its GRAS domain. Recent studies showed that DELLA stability is regulated post-translationally via two mechanisms, phytohormone gibberellin-induced polyubiquitination for its rapid degradation, and Small Ubiquitin-like Modifier (SUMO)-conjugation to alter its accumulation. Moreover, DELLA activity is dynamically modulated by two distinct glycosylations: DELLA-TF interactions are enhanced by O-fucosylation, but inhibited by O-linked N-acetylglucosamine (O-GlcNAc) modification. However, the role of DELLA phosphorylation remains unclear. Here, we identified phosphorylation sites in REPRESSOR OF ga1-3 (RGA, an AtDELLA) purified from Arabidopsis by tandem mass spectrometry analysis, and showed that phosphorylation of the RGA LKS-peptide in the poly-S/T region enhances RGA-H2A interaction and RGA association with target promoters. Interestingly, phosphorylation does not affect RGA-TF interactions. Our study has uncovered that phosphorylation is a new regulatory mechanism of DELLA activity.
2024-08-08 | PXD046004 | Pride
Project description:The PFYRE Subdomain in Master Growth Repressor DELLA is Essential for Its Association with Target Chromatin via Histone H2A Binding
| PRJNA975081 | ENA
Project description:DELLA proteins are conserved master growth regulators that play a central role in controlling plant development in response to internal and environmental cues. DELLAs function as transcription regulators, which are recruited to target promoters by binding to transcription factors (TFs) and histone H2A via their GRAS domain. Recent studies showed that DELLA stability is regulated post-translationally via two mechanisms, phytohormone gibberellin-induced polyubiquitination for its rapid degradation, and Small Ubiquitin-like Modifier (SUMO)-conjugation to increase its accumulation. Moreover, DELLA activity is dynamically modulated by two distinct glycosylations: DELLA-TF interactions are enhanced by O-fucosylation, but inhibited by O-linked N-acetylglucosamine (O-GlcNAc) modification. However, the role of DELLA phosphorylation remains unclear as previous studies showing conflicting results ranging from findings that suggest phosphorylation promotes or reduces DELLA degradation to others indicating it has no effect on its stability. Here, we identify phosphorylation sites in REPRESSOR OF ga1-3 (RGA, an AtDELLA) purified from Arabidopsis by mass spectrometry analysis, and show that phosphorylation of two RGA peptides in the PolyS and PolyS/T regions enhances RGA activity by promoting H2A binding and RGA association with target promoters. Notably, phosphorylation does not affect RGA-TF interactions or RGA stability. Our study has uncovered a molecular mechanism of phosphorylation-induced DELLA activity.
| S-EPMC11372120 | biostudies-literature
Project description:The diterpenoid phytohormone gibberellin (GA) controls diverse developmental processes throughout the plant life cycle. DELLA proteins are master growth repressors that function immediately downstream of the GA receptor to inhibit GA signaling. By doing so, DELLAs also play pivotal roles as integrators of internal developmental signals from multiple hormone pathways and external cues. DELLAs are likely nuclear transcriptional regulators, which interact with other transcription factors to modulate expression of GA-responsive genes. DELLAs are also involved in maintaining GA homeostasis through feedback up-regulating expression of GA biosynthesis and receptor genes. However, the molecular mechanisms by which DELLAs restrict growth and development are largely unknown. This study reveals an important step of the mechanism. Previous microarray studies identified scarecrow-like 3 (SCL3) as a direct target gene of DELLA in Arabidopsis seedlings. SCL3 expression is induced by DELLA and repressed by GA. Unexpectedly, a scl3 null mutant displays reduced GA responses and elevated expression of GA biosynthesis genes during seed germination and seedling growth, indicating that SCL3 functions as a positive regulator of GA signaling. SCL3 seems to act as an attenuator of DELLA proteins. Transient expression, ChIP, and co-IP studies show that SCL3 autoregulates its own transcription by directly interacting with DELLA. Our data further show that SCL3 and DELLA antagonize each other in controlling both downstream GA responses and upstream GA biosynthetic genes. This work is beginning to shed light on how this complex regulatory network achieves GA homeostasis and controls GA-mediated growth and development in the plant.
| S-EPMC3033277 | biostudies-literature
Project description:The aim of this study is to identify early DELLA protein-responsive genes using a Dexamethasone (DEX)-inducible system. Two transgenic lines were used: one induces the expression of a dominant, gibberellin non-responsive DELLA protein (rga-delta17); the other is a control line that carries the same vector, but lacks the rga-delta17 transgene. By comparing the gene expression changes in the line that expresses the rga-delta17 protein in the presence or absence of DEX it is possible to identify putative targets of DELLA proteins. An empty vector transgenic line was included in this study to identify genes that might be regulated by the DEX inducible system that are not dependent on the DELLA protein. Keywords: Dexamethasone treatment, gibberellin treatment, time course, transgene effect
2007-11-21 | GSE8741 | GEO
Project description:Transcriptome changes 1h or 4h following DELLA stabilisation in microdissected fully proliferating Arabidopsis leaves
2013-08-01 | GSE49399 | GEO
Project description:The DELLA family of transcription regulators functions as master growth repressors in plants by inhibiting phytohormone gibberellin (GA) signaling in response to developmental and environmental cues. DELLAs also play a central role in mediating cross-talk between GA and other signaling pathways via antagonistic direct interactions with key transcription factors. However, how these crucial protein-protein interactions can be dynamically regulated during plant development remains unclear. Here, we show that DELLAs are modified by the O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) SECRET AGENT (SEC) in Arabidopsis. O-GlcNAcylation of the DELLA protein REPRESSOR OF ga1-3 (RGA) inhibits RGA binding to four of its interactors-PHYTOCHROME-INTERACTING FACTOR3 (PIF3), PIF4, JASMONATE-ZIM DOMAIN1, and BRASSINAZOLE-RESISTANT1 (BZR1)-that are key regulators in light, jasmonate, and brassinosteroid signaling pathways, respectively. Consistent with this, the sec-null mutant displayed reduced responses to GA and brassinosteroid and showed decreased expression of several common target genes of DELLAs, BZR1, and PIFs. Our results reveal a direct role of OGT in repressing DELLA activity and indicate that O-GlcNAcylation of DELLAs provides a fine-tuning mechanism in coordinating multiple signaling activities during plant development.
| S-EPMC4719307 | biostudies-literature
Project description:rs09-09_della-dark - della-regulation in darkness versus light - Identification of DELLA-dependent downstream targets in darkness - Aim was to determine downstream target of DELLA proteins involved in skotomorphogenesis. Wt, ga1-3, ga1-3_rga_gai_rgl1_rgl2_rgl3 global seeds were sterilized, sown on MS agar plates then put for stratification for 3 days at 4°C. Plates were placed in growth cabinet at 22°C for 5 days in darkness or in continous light. Keywords: gene knock out
2011-06-13 | GSE22681 | GEO