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

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

PROVIDER: PRJNA1205737 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31876605_1.fastq.gz	Fastqsanger.gz
	SRR31876605_2.fastq.gz	Fastqsanger.gz
	SRR31876606_1.fastq.gz	Fastqsanger.gz
	SRR31876606_2.fastq.gz	Fastqsanger.gz
	SRR31876607_1.fastq.gz	Fastqsanger.gz

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

Project description:RNA-seq anaysis compares gene expression of the asp1-H397A aps1∆ siw14∆ spx1∆ (HASX) mutant to the wild-type fission yeast (Schizosaccharomyces pombe)

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

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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

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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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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

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

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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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