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Molecular basis of GA-independent DELLA regulation by the VIH-type inositol pyrophosphate synthase in a non-vascular land plant

ABSTRACT: Molecular basis of GA-independent DELLA regulation by the VIH-type inositol pyrophosphate synthase in a non-vascular land plant

PROVIDER: PRJNA1121321 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29324661_1.fastq.gz	Fastqsanger.gz
	SRR29324661_2.fastq.gz	Fastqsanger.gz
	SRR29324662_1.fastq.gz	Fastqsanger.gz
	SRR29324662_2.fastq.gz	Fastqsanger.gz
	SRR29324663_1.fastq.gz	Fastqsanger.gz

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Molecular basis of GA-independent DELLA regulation by the VIH-type inositol pyrophosphate synthase in a non-vascular land plant

Project description:To study the functional relationship between MpVIH and MpDELLA at molecular level, the system-wide transcriptome profile of the following genotype were analysed: WT, CRISPR/Cas9 knockout lines of MpVIH (Mpvih) and independent Mpvih transgenic lines with reduced MpDELLA transcripts using an artificial microRNA (Mpvih::amiR-MpDELLA) technology.

2025-05-21 | GSE269387 | GEO

Inositol pyrophosphate dynamics impact fission yeast phosphate homeostasis via modulation of RNA 3' processing and transcription termination

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Chromatin mechanism of DELLA-mediated gene repression and Gibberellin-induced gene activation in rice

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Tandem inactivation of inositol pyrophosphatases illuminates distinct etiologies of inositol pyrophosphate toxicosis in fission yeast

Project description:Tandem inactivation of inositol pyrophosphatases illuminates distinct etiologies of inositol pyrophosphate toxicosis in fission yeast

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Inositol pyrophosphate InsP8 acts as intracellular phosphate signal in Arabidopsis

Project description:Inositol pyrophosphate InsP8 acts as intracellular phosphate signal in Arabidopsis

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Inositol pyrophosphate InsP8 acts as intracellular phosphate signal in Arabidopsis

Project description:The maintenance of cellular phosphate (Pi) homeostasis is of paramount importance in living organisms. Little is known about how cells sense intracellular Pi status in multi-cellular eukaryotes. Here, we report the identification of inositol pyrophosphate InsP8, a ligand that binds to the Pi sensor protein SPX1 to inhibit PHR1, the central regulator of Pi starvation responses in Arabidopsis. The concentration of InsP8, synthesized by diphosphoinositol pentakisphosphate kinases VIH1 and VIH2, depends on cellular Pi level and the double mutants accumulated higher amounts of Pi. The paradox of Pi toxicity and induction of Pi starvation inducible genes indicated that the cells could not sense cellular Pi without InsP8. Our study reveals that InsP8 acts as a Pi signaling molecule and binds to the receptor SPX1 to regulate Pi homeostasis.

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Expression data from leaves of GA-deficient and GA-insensitive transgenic poplar

Project description:We used whole-genome microarrays to identify differentially expressed genes in leaves of GA-deficient (35S::PcGA2ox) and/or GA-insensitive (35S::rgl1) transgenics as compared to WT poplar (717-1B4 genotype). Our work suggests that the molecular machinery that reduces gibberellins (GAs) concentration and signaling is a major route for restraining growth under both immediate and imminent adverse conditions. We show that inhibition of growth as a result of water deprivation and short days (SDs) coincides with up-regulation of several DELLA and GA2ox encoding genes in poplar. Likewise, GA-deficient and GA-insensitive transgenics, with up-regulated GA2ox and DELLA domain proteins, elicited a hypersensitive growth inhibition in response to both drought and SDs. Because the GA-modified transgenic showed accelerated response to drought and SD, we hypothesized that the mechanisms associated with these responses are constitutively elevated even under control conditions (well-watered, long day photoperiod). Therefore, we used whole-genome poplar microarray to study transcriptome level changes in the leaves of transgenic compared to WT plants grown under control environment.

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INDETERMINATE DOMAIN-DELLA protein interactions orchestrate gibberellin-mediated cell elongation in wheat and barley

Project description:DELLA proteins are members of the GRAS-domain family of transcriptional regulators and modulate transcriptional activity through protein-protein interactions with at least 15 different classes of transcription factor. The plant hormone gibberellin (GA) regulates a range of growth and development responses including promoting cell elongation, by triggering the degradation of DELLA proteins. More than 70% of modern wheat (Triticum aestivum L.) varieties carry alleles encoding DELLA proteins that are resistant to GA-mediated degradation. These alleles result in constitutive growth repression in stem tissues and confer a semi-dwarf growth habit associated with improved lodging resistance. However, these alleles also have negative pleiotropic effects such as reduced nitrogen use efficiency and weak early vigour that restrict their utility in some environments. A detailed understanding of the mechanisms by which DELLA proteins regulate growth and development will be necessary to dissect these responses and develop targeted strategies to breed improved crop varieties. We identified the orthologous C2H2 Zinc-finger transcription factors INDETERMINATE DOMAIN 5 (IDD5) in wheat and SEMI-DWARF3 (SDW3) in barley (Hordeum vulgare) as positive regulators of stem and leaf expansion. Both IDD5 and SDW3 physically interact with DELLA proteins and are epistatic to these genes. We propose a mechanism by which IDD proteins integrate GA signals to modulate downstream gene transcriptional activity through a protein complex dual activation and repression activities. Changes in GA biosynthesis gene expression levels suggest that part of this response involves GA homeostasis. Plants carrying null mutations in IDD5 and SDW3 exhibit a GA-insensitive semi-dwarf growth habit comparable to the Rht-D1b ‘Green Revolution’ allele and have potential as novel dwarfing alleles in cereal breeding programmes.

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SPX domain proteins are agents of inositol pyrophosphate toxicosis in fission yeast

Project description:SPX domain proteins are agents of inositol pyrophosphate toxicosis in fission yeast

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A GAF domain mediates inositol pyrophosphate substrate channeling in PPIP5K phosphatases

Project description:Inositol pyrophosphates are highly phosphorylated nutrient messengers. The final step of their biosynthesis is catalyzed by diphosphoinositol pentakisphosphate kinase (PPIP5K) enzymes, which are conserved among fungi, plants, and animals. PPIP5Ks contain an N-terminal kinase domain that generates the active messenger 1,5-InsP8 and a C-terminal phosphatase domain that participates in PP-InsP catabolism. The balance between kinase and phosphatase activities controls the cellular levels and signaling capacity of 1,5- InsP8. Here, we present crystal structures of the apo and substrate-bound Vip1 phosphatase domain from S. cerevisiae (ScVip1PD). ScVip1PD is a phytase-like inositol 1-pyrophosphate phosphatase with two conserved histidine phosphatase catalytic motifs. The enzyme has a strong preference for 1,5-InsP8 and is inhibited by inorganic phosphate. ScVip1PD has an α-helical insertion domain stabilized by a structural Zn2+ binding site, and a unique GAF domain that exists in an open and closed state, allowing channeling of the 1,5-InsP 8 substrate to the active site. Mutations that alter the active site, that restrict the movement of the GAF domain or that modify the charge of the substrate channel significantly inhibit the activity of the yeast enzyme in vitro, and the function of the Arabidopsis PPIP5K VIH2 in planta. Structural analyses of full-length PPIP5Ks suggest that the kinase and phosphatase are independent enzymatic modules. Taken together, our work reveals the structure, enzymatic mechanism and regulation of eukaryotic PPIP5K phosphatases

2024-10-07 | PXD056020 | Pride

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