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A plastidial lipoyl synthase LIP1p plays a crucial role in phosphate homeostasis in Arabidopsis

ABSTRACT: A plastidial lipoyl synthase LIP1p plays a crucial role in phosphate homeostasis in Arabidopsis

PROVIDER: PRJNA1133686 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29755816_1.fastq.gz	Fastqsanger.gz
	SRR29755816_2.fastq.gz	Fastqsanger.gz
	SRR29755817_1.fastq.gz	Fastqsanger.gz
	SRR29755817_2.fastq.gz	Fastqsanger.gz
	SRR29755818_1.fastq.gz	Fastqsanger.gz

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A plastidial lipoyl synthase LIP1p plays a crucial role in phosphate homeostasis in Arabidopsis.

Project description:A plastidial lipoyl synthase LIP1p plays a crucial role in phosphate homeostasis in Arabidopsis.

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A plastidial lipoyl synthase LIP1p plays a crucial role in phosphate homeostasis in Arabidopsis.

Project description:Phosphate (Pi) homeostasis is important for plant growth and adaptation to dynamic environment, which requires the precise regulation of phosphate transporter (PHT) trafficking from endoplasmic reticulum to plasma membrane. LIPOYL SYNTHASE 1p (LIP1p) is known as a key enzyme in plastids to catalyze lipoylation of pyruvate dehydrogenase complex for de novo fatty acid synthesis. It is unknown whether this process is involved in regulating Pi homeostasis. Here, we demonstrate a new role of LIP1p in controlling Pi homeostasis by regulating PHT1 trafficking. We recovered a weak mutant allele of LIP1p in Arabidopsis that accumulates much less Pi and has enhanced expression of phosphate starvation induced genes. Lipidomics analysis revealed that LIP1p mutation alters lipid profile and compromises vesicle trafficking of PHT1 to the plasma membrane to impair Pi uptake. Beside phosphorus, the homeostasis of a series of mineral nutrients was also perturbed in lip1p mutant. Our findings provide powerful genetic evidences to support the linkage between lipoylation and ion homeostasis in plant.

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A plastidial lipoyl synthase LIP1p plays a crucial role in phosphate homeostasis in Arabidopsis

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Project description:Proteins incorporating iron-sulfur (Fe-S) cofactors are required for a plethora of metabolic processes. Their maturation depends on three Fe-S cluster assembly machineries located in the cytosol, mitochondria and chloroplasts. After de novo formation on scaffold proteins, Fe-S centers are loaded on client proteins by use of Fe-S cluster transfer proteins. Among plastidial representatives of this latter category, NFU2 and NFU3 are required for the maturation of the [4Fe-4S] clusters found in photosystem I subunits acting upstream of HCF101. NFU2 is additionally required for the maturation of the [2Fe-2S] dihydroxyacid dehydratase, important for branched-chain amino acid synthesis. Here, we report that recombinant Arabidopsis thaliana NFU1 is able to solely assemble a [4Fe-4S] cluster per homodimer. We also provide insights into the specificity of NFU1 for the maturation of chloroplastic Fe-S proteins by performing co-immunoprecipitation experiments and assaying the physical interaction of NFU1 with many [4Fe-4S]-containing plastidial proteins using binary yeast two-hybrid assays. Interactions with two proteins involved in isoprenoid and thiamine biosynthesis, respectively 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase (ISPG) and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase (THIC), have been further confirmed by bimolecular fluorescence complementation and in vitro Fe-S cluster transfer experiments. The additional interactions detected with SUFD and SUFA allowed building a model in which NFU1 receives its Fe-S cluster from the SUFBC2D scaffold complex and serves for the maturation of [4Fe-4S] client proteins.

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