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Inositol pyrophosphate InsP8 acts as intracellular phosphate signal in Arabidopsis

ABSTRACT: Inositol pyrophosphate InsP8 acts as intracellular phosphate signal in Arabidopsis

PROVIDER: PRJNA523789 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8608730_1.fastq.gz	Fastqsanger.gz
	SRR8608730_2.fastq.gz	Fastqsanger.gz
	SRR8608725_1.fastq.gz	Fastqsanger.gz
	SRR8608725_2.fastq.gz	Fastqsanger.gz
	SRR8608726_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

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.

2022-02-22 | GSE126927 | GEO

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

Project description:This RNA-Seq analysis compares gene expression of the Inositol pyrophosphate phosphatase mutant aps1∆ and Inositol pyrophsophate kinase mutant asp1-D333A contrasting to the WT in the fission yeast S. pombe

2019-06-16 | GSE131237 | GEO

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

Project description:Inositol pyrophosphate dynamics impact phosphate homeostasis via modulation of RNA 3' processing and transcription termination

| PRJNA524918 | ENA

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

| PRJNA769102 | ENA

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

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

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

| PRJNA543029 | ENA

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

Project description:Fission yeast phosphate acquisition genes pho1, pho84, and tgp1 are repressed in phosphate-rich medium by transcription of upstream lncRNAs. Here we show phosphate homeostasis is subject to metabolite control by inositol pyrophosphates (IPPs), exerted through the 3'-processing/termination machinery and the Pol2 CTD code. Increasing IP8 (via Asp1 IPP pyrophosphatase mutation) de-represses the PHO regulon and leads to precocious termination of prt lncRNA synthesis. pho1 de-repression by IP8 depends on cleavage-polyadenylation factor (CPF) subunits, termination factor Rhn1, and the Thr4 letter of the CTD code. pho1 de-repression by mutation of the Ser7 CTD letter depends on IP8. Simultaneous inactivation of Asp1 and Aps1 pyrophosphatases (i.e., too much IP8) is lethal, but this lethality is suppressed by mutations of CPF subunits Ppn1, Swd22, Ssu72, and Ctf1 and CTD mutation T4A. Failure to synthesize IP8 (via Asp1 IPP kinase mutation) results in pho1 hyper-repression. Synthetic lethality of asp1∆ with Ppn1, Swd22, and Ssu72 mutations argues that IP8 plays an important role in essential 3'-processing/termination events, albeit in a manner genetically redundant to CPF. Transcriptional profiling delineates an IPP-responsive regulon composed of genes overexpressed when IP8 levels are increased. Our results establish a novel role for IPPs in cell physiology.

2019-06-16 | GSE127550 | GEO

Inositol signaling in the basidiomycete fungus Schizophyllum commune

Project description:Intracellular signaling is conserved in eukaryotes to allow for response to extracellular signals and to regulate development and cellular functions. In fungi, inositol phosphate signaling has been shown to be involved in growth, sexual reproduction, and metabolic adaptation lacking, however, reports of mushroom forming fungi so far. In Schizophyllum commune, an inositol monophosphatase has been found up-regulated during sexual development. The enzyme is crucial for inositol cycling where it catalyzes the last step of inositol phosphate metabolism restoring the inositol pool from the monophosphorylated inositol monophosphate. We overexpressed the gene in this model basidiomycete and verified its involvement in cell wall integrity and intracellular trafficking. Strong phenotypes in mushroom formation and cell metabolism were evidenced by proteome analyses. In addition, altered inositol signaling was shown to be involved in tolerance towards cesium and zinc, and increased metal tolerance towards cadmium, associated with induced expression of kinases and repression of phosphatases within the inositol cycle. The presence of the heavy metals Sr, Cs, Cd, and Zn lowered intracellular calcium levels. We could develop a model integrating inositol signaling in the known signal transduction pathways governed by Ras, G-protein coupled receptors, cAMP and elucidate different roles in development.

2021-07-01 | PXD026465 | Pride

Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding.

Project description:Inositol pyrophosphates (such as IP7 and IP8) are multifunctional signaling molecules that regulate diverse cellular activities. Inositol pyrophosphates have 'high-energy' phosphoanhydride bonds, so their enzymatic synthesis requires that a substantial energy barrier to the transition state be overcome. Additionally, inositol pyrophosphate kinases can show stringent ligand specificity, despite the need to accommodate the steric bulk and intense electronegativity of nature's most concentrated three-dimensional array of phosphate groups. Here we examine how these catalytic challenges are met by describing the structure and reaction cycle of an inositol pyrophosphate kinase at the atomic level. We obtained crystal structures of the kinase domain of human PPIP5K2 complexed with nucleotide cofactors and either substrates, product or a MgF(3)(-) transition-state mimic. We describe the enzyme's conformational dynamics, its unprecedented topological presentation of nucleotide and inositol phosphate, and the charge balance that facilitates partly associative in-line phosphoryl transfer.

| S-EPMC3923263 | biostudies-literature

Two bifunctional inositol pyrophosphate kinases/phosphatases control plant phosphate homeostasis.

Project description:Many eukaryotic proteins regulating phosphate (Pi) homeostasis contain SPX domains that are receptors for inositol pyrophosphates (PP-InsP), suggesting that PP-InsPs may regulate Pi homeostasis. Here we report that deletion of two diphosphoinositol pentakisphosphate kinases VIH1/2 impairs plant growth and leads to constitutive Pi starvation responses. Deletion of phosphate starvation response transcription factors partially rescues vih1 vih2 mutant phenotypes, placing diphosphoinositol pentakisphosphate kinases in plant Pi signal transduction cascades. VIH1/2 are bifunctional enzymes able to generate and break-down PP-InsPs. Mutations in the kinase active site lead to increased Pi levels and constitutive Pi starvation responses. ATP levels change significantly in different Pi growth conditions. ATP-Mg2+ concentrations shift the relative kinase and phosphatase activities of diphosphoinositol pentakisphosphate kinases in vitro. Pi inhibits the phosphatase activity of the enzyme. Thus, VIH1 and VIH2 relay changes in cellular ATP and Pi concentrations to changes in PP-InsP levels, allowing plants to maintain sufficient Pi levels.

| S-EPMC6731061 | biostudies-literature

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