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

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

PROVIDER: PRJNA769102 | ENA |

REPOSITORIES: ENA

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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

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

Project description:This RNA-Seq analysis compares gene expression of spx1∆ mutant contrasting to the WT fission yeast S. pombe

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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

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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.

2022-02-22 | GSE126927 | 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

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Cleavage-Polyadenylation Factor Cft1 and SPX Domain Proteins Are Agents of Inositol Pyrophosphate Toxicosis in Fission Yeast.

Project description: Not available

| S-EPMC8749416 | biostudies-literature

Genetic suppressor screen identifies Tgp1 (glycerophosphocholine transporter), Plc1 (phospholipase C), and Kcs1 (IP6 kinase) as determinants of inositol pyrophosphate toxicosis in fission yeast

Project description:RNA-seq analysis compares gene expression of the STF6 (asp1-W386*), STF9 (asp1-W493*), kcs1-R332T, kcs1-L338R, and kcs1-E834K mutants to the wild-type fission yeast (Schizosaccharomyces pombe).

2023-12-05 | GSE241189 | GEO

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

Suppression of inositol pyrophosphate toxicosis and hyper-repression of the fission yeast PHO regulon by loss-of-function mutations in chromatin remodelers Snf22 and Sol1

Project description:RNA-seq analysis compares gene expression of the snf22∆ and snf22-(D996A-E997A) mutants to the wild-type fission yeast (Schizosaccharomyces pombe).

2024-04-22 | GSE245138 | GEO

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