Dataset Information

Phosphate and phosphite differentially impact the proteome and phosphoproteome of Arabidopsis suspension cell cultures

ABSTRACT: Phosphorus is an essential limited nutrient for plant growth and modern agricultural productivity. A comprehensive understanding of how plants respond to phosphate starvation is essential to develop more phosphate-use efficient crops. Here we quantified protein-level responses to phosphate (PO4-) and phosphite (PO3-) in Arabidopsis thaliana suspension cells, relative to a phosphate-starved state using label-free proteomics and phosphoproteomics. Phosphite is similarly sensed and taken up by plants as phosphate but cannot be used as a source of phosphorus. Phosphite is hence a useful tool to delineate between non-specific processes related to sensing and transport, and specific responses to phosphorus nutrition. We find that responses to phosphate and phosphite occur mainly at the level of protein phosphorylation, complemented by limited changes in protein abundance, primarily in protein translation, and phosphate transport and scavenging proteins. Phosphorylation changes in proteins involved in core processes such as translation, RNA splicing and kinase signalling are especially important in phosphate starvation. We also find differential phosphorylation in response to phosphate and phosphite in 69 proteins, including splicing factors, translation factors, the PHT1;4 phosphate transporter and the HAT1 histone acetyltransferase—potential phospho-switches sensing changes in phosphorus nutrition. Our study hence illuminates several new aspects of the phosphate-starvation response and identifies important targets for further investigation and crop improvement.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Cell Suspension Culture

SUBMITTER: Richard Uhrig

LAB HEAD: Richard Uhrig

PROVIDER: PXD018989 | Pride | 2021-01-04

REPOSITORIES: Pride

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Publications

Phosphate and phosphite have a differential impact on the proteome and phosphoproteome of Arabidopsis suspension cell cultures.

Mehta Devang D Ghahremani Mina M Pérez-Fernández Maria M Tan Maryalle M Schläpfer Pascal P Plaxton William C WC Uhrig R Glen RG

The Plant journal : for cell and molecular biology 20201219 4

Phosphorus absorbed in the form of phosphate (H2 PO4- ) is an essential but limiting macronutrient for plant growth and agricultural productivity. A comprehensive understanding of how plants respond to phosphate starvation is essential for the development of more phosphate-efficient crops. Here we employed label-free proteomics and phosphoproteomics to quantify protein-level responses to 48 h of phosphate versus phosphite (H2 PO3- ...[more]

PMID: 33184936

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Project description:The Chlamydomonas reinhardtii transcription factor PSR1 is required for the control of activities involved in scavenging phosphate from the environment during periods of phosphorus limitation. Increased scavenging activity reflects the development of high-affinity phosphate transport and the expression of extracellular phosphatases that can cleave phosphate from organic compounds in the environment. A comparison of gene expression patterns using microarray analyses and quantitative PCRs with wild-type and psr1 mutant cells deprived of phosphorus has revealed that PSR1 also controls genes encoding proteins with potential "electron valve" functions--these proteins can serve as alternative electron acceptors that help prevent photodamage caused by overexcitation of the photosynthetic electron transport system. In accordance with this finding, phosphorus-starved psr1 mutants die when subjected to elevated light intensities; at these intensities, the wild-type cells still exhibit rapid growth. Acclimation to phosphorus deprivation also involves a reduction in the levels of transcripts encoding proteins involved in photosynthesis and both cytoplasmic and chloroplast translation as well as an increase in the levels of transcripts encoding stress-associated chaperones and proteases. Surprisingly, phosphorus-deficient psr1 cells (but not wild-type cells) also display expression patterns associated with specific responses to sulfur deprivation, suggesting a hitherto unsuspected link between the signal transduction pathways involved in controlling phosphorus and sulfur starvation responses. Together, these results demonstrate that PSR1 is critical for the survival of cells under conditions of suboptimal phosphorus availability and that it plays a key role in controlling both scavenging responses and the ability of the cell to manage excess absorbed excitation energy. Set of arrays that are part of repeated experiments Biological Replicate Computed

Dataset Information

Phosphate and phosphite differentially impact the proteome and phosphoproteome of Arabidopsis suspension cell cultures

Publications

Phosphate and phosphite have a differential impact on the proteome and phosphoproteome of Arabidopsis suspension cell cultures.

Similar Datasets

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