ArticlePlant signaling & behavior2012
A specific variant of the PHR1 binding site is highly enriched in the Arabidopsis phosphate-responsive phospholipase DZ2 coexpression network.
Article in Plant signaling & behavior, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- A Role for Inositol Pyrophosphates in the Metabolic Adaptations to Low Phosphate inMetabolites · 2021Article
- SPX4 Acts on PHR1-Dependent and -Independent Regulation of Shoot Phosphorus Status in Arabidopsis.Plant physiology · 2019Article
- A phosphate starvation-driven bidirectional promoter as a potential tool for crop improvement and in vitro plant biotechnology.Plant biotechnology journal · 2017Article
- Lipid biosynthesis and protein concentration respond uniquely to phosphate supply during leaf development in highly phosphorus-efficient Hakea prostrata.Plant physiology · 2014Article
- Differential regulation of two types of monogalactosyldiacylglycerol synthase in membrane lipid remodeling under phosphate-limited conditions in sesame plants.Frontiers in plant science · 2013Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PLDZ2 is a member of the Arabidopsis phospholipase D gene family that is induced in both shoot and root in response to phosphate (Pi) starvation. Recently, through deletion and gain-of-function analyses of the PLDZ2 promoter, we identified a 65 bp region (denominated enhancer EZ2) capable of conferring tissue-specific and low-Pi responses to a minimal inactive promoter. The EZ2 element contains two P1BS motifs, each of which is the binding site for PHR1 and related transcription factors. This structural organization is evolutionarily conserved in orthologous promoters within the rosid clade. To determine whether EZ2 is significantly over-represented in Arabidopsis genes coexpressed with PLDZ2, we constructed a PLDZ2 coexpression network containing 26 genes, almost half of them encoding enzymes or regulatory proteins involved in Pi recycling. A variant of the P1BS motif was found to be highly enriched in the promoter regions of these coexpressed genes, showing an EZ2-like arrangement in seven of them. No other motifs were significantly enriched. The over-representation of the EZ2 arrangement of P1BS motifs in the promoters of genes coexpressed with PLDZ2, suggests this unit has a particularly important role as a regulatory element in a coexpression network involved in the release of Pi from phospholipids and other molecules under Pi-limiting conditions.
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