Keep an Eye on PPi: The Vacuolar-Type H+-Pyrophosphatase Regulates Postgerminative Development in<i>Arabidopsis</i>

Ferjani, Ali; Segami, Shoji; Horiguchi, Gorou; Muto, Yukari; Maeshima, Masayoshi; Tsukaya, Hirokazu

doi:10.1105/tpc.111.085415

Cited by 147 publications

(328 citation statements)

References 63 publications

Supporting

Mentioning

316

Contrasting

Order By: Relevance

“…Previously, it was reported that the null mutants fugu5-1, fugu5-2, and fugu5-3 have an increased PPi concentration in the cytosol. This increased concentration has a visibly negative impact on the development of cotyledons and hypocotyl elongation in etiolated seedlings, due to metabolic inhibition of key enzymes by PPi overload (Ferjani et al, 2011). We compared the cotyledon growth of the triple KO mutant to the three fugu5 alleles but did not observe the typical elongated shape of cotyledons in AVP1 mutants (Fig.…”

Section: Triple Ko Mutant Does Not Mimic or Amplify Phenotypes Causedmentioning

confidence: 99%

“…7A). As previously described, the fugu5-1 line complemented with the yeast IPP1 soluble pyrophosphatase developed normal cotyledons (Ferjani et al, 2011). In addition, we combined the ppspase1-1 and pecp1-1 mutations with the fugu5-1 allele to determine whether combining the three mutations could enhance the elongated cotyledon phenotype or lead to a new phenotype (Fig.…”

Section: Triple Ko Mutant Does Not Mimic or Amplify Phenotypes Causedmentioning

confidence: 99%

Section: Triple Ko Mutant Does Not Mimic or Amplify Phenotypes Causedmentioning

confidence: 99%

“…Considering that PPsPase1 and PECP1 are strongly expressed in the vascular tissues, future research should examine how these mutations affect the content of PCho in the xylem sap. Analysis of KO mutants and overexpressing lines also revealed that these enzymes strongly affect PEth content in plants, demonstrating that both PCho and PEth can be used as substrates by PPsPase1 and PECP1.As for PPi degradation, there was no indication of PPi imbalance when our mutants were compared to or combined with known PPi-degradation defective mutants (fugu5; Ferjani et al, 2011). While it has been suggested that alternative pathways using PPi as an energy source could be an essential strategy for plants to withstand Pi starvation (Plaxton and Tran, 2011), PPsPase1 and PECP1 do not appear to significantly affect this process.…”

mentioning

confidence: 99%

“…We therefore performed several assays to verify these activities in planta. As PPi quantification is notoriously challenging (Gdula et al, 1998;Heinonen, 2001), we opted for a more physiological approach to compare our mutants to previously described mutant lines impaired in their cytosolic PPi concentration (Ferjani et al, 2011).The fugu5 mutant lines are deficient in AVP1, a PPi-dependent proton pump (Ferjani et al, 2011;Pizzio et al, 2015). Previously, it was reported that the null mutants fugu5-1, fugu5-2, and fugu5-3 have an increased PPi concentration in the cytosol.…”

mentioning

confidence: 99%

See 4 more Smart Citations

The Phosphate Fast-Responsive Genes PECP1 and PPsPase1 Affect Phosphocholine and Phosphoethanolamine Content

et al. 2018

Self Cite

View full text Add to dashboard Cite

Phosphate starvation-mediated induction of the HAD-type phosphatases PPsPase1 (AT1G73010) and PECP1 (AT1G17710) has been reported in Arabidopsis (Arabidopsis thaliana). However, little is known about their in vivo function or impact on plant responses to nutrient deficiency. The preferences of PPsPase1 and PECP1 for different substrates have been studied in vitro but require confirmation in planta. Here, we examined the in vivo function of both enzymes using a reverse genetics approach. We demonstrated that PPsPase1 and PECP1 affect plant phosphocholine and phosphoethanolamine content, but not the pyrophosphate-related phenotypes. These observations suggest that the enzymes play a similar role in planta related to the recycling of polar heads from membrane lipids that is triggered during phosphate starvation. Altering the expression of the genes encoding these enzymes had no effect on lipid composition, possibly due to compensation by other lipid recycling pathways triggered during phosphate starvation. Furthermore, our results indicated that PPsPase1 and PECP1 do not influence phosphate homeostasis, since the inactivation of these genes had no effect on phosphate content or on the induction of molecular markers related to phosphate starvation. A combination of transcriptomics and imaging analyses revealed that PPsPase1 and PECP1 display a highly dynamic expression pattern that closely mirrors the phosphate status. This temporal dynamism, combined with the wide range of induction levels, broad expression, and lack of a direct effect on Pi content and regulation, makes PPsPase1 and PECP1 useful molecular markers of the phosphate starvation response.Plant growth is highly sensitive to a lack of phosphate (Pi); hence, the application of Pi fertilizers has become standard practice for high-throughput crop production (Cordell et al., 2009). Most phosphorus in the soil is not available to plants, as it is combined with other minerals or parts of organic compounds (Bieleski, 1973;Raghothama and Karthikeyan, 2005). Only a small fraction of soluble Pi (usually present at a concentration of ,10 mM in the soil) can be taken up by plants.Although growth is not optimal under limiting conditions, plants can withstand changing Pi concentrations within heterogeneous soils or in the external nutrient supply that can lead to reprogramming of their metabolism and architecture (Hammond et al., 2003;Péret et al., 2011;Plaxton and Tran, 2011). Root architecture can be modified to facilitate Pi uptake by favoring the development of lateral roots (at the expense of primary root elongation in many plants including Arabidopsis), increasing the density and length of root hairs, and limiting the development of aerial parts (López-Bucio et al., 2002;Svistoonoff et al., 2007;Gruber et al., 2013). Pi uptake mechanisms are enhanced at the root/soil interface, particularly through the stimulation of Pi transport activity (Mudge et al., 2002;Shin et al., 2004;Nussaume et al., 2011; Ayadi et al., 2015). In parallel, mobilization of Pi sources fr...

show abstract

Section: Triple Ko Mutant Does Not Mimic or Amplify Phenotypes Causedmentioning

confidence: 99%

Section: Triple Ko Mutant Does Not Mimic or Amplify Phenotypes Causedmentioning

confidence: 99%

Section: Triple Ko Mutant Does Not Mimic or Amplify Phenotypes Causedmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

The Phosphate Fast-Responsive Genes PECP1 and PPsPase1 Affect Phosphocholine and Phosphoethanolamine Content

et al. 2018

Self Cite

View full text Add to dashboard Cite

show abstract

Plant Vacuoles

Rea

2018

Encyclopedia of Life Sciences

View full text Add to dashboard Cite

Vacuoles can represent 90% or more of the total volume of a mature plant cell. Derived from the endoplasmic reticulum and Golgi complex and delimited from the cytosol by the vacuolar membrane (tonoplast), they are versatile dynamic organelles capable of assuming different morphologies and serving a wide range of functions in different cells or in the same cells at different times. Many cells contain just one central vacuole, others contain several that differ in their relative contributions to lytic and storage functions and a few contain compound vacuoles – vacuoles within vacuoles – by means of which lytic and storage functions are partitioned within a single vacuole. The many processes in which vacuoles participate include the maintenance of tissue water balance and turgor regulation for growth, mechanical support, stomatal aperture control and thigmotropic responses; inorganic and organic nutrient storage and retrieval; macromolecule turnover and salvage; cytosolic inorganic ion and metabolite homeostasis; storage excretion and detoxification of endogenous waste products, heavy metals and other xenobiotics. Although most of the carrier‐ or channel‐mediated transport processes that occur across the vacuolar membrane are driven by the H + electrochemical gradient (proton motive force, PMF) established by ATP (adenosine triphosphate)‐energised V‐type H + ‐ATPases and inorganic pyrophosphate‐energised H + ‐PPases (V‐PPase), there are many that are directly energised by ATP through the action of P‐type ATPases or ATP‐binding cassette (ABC) transporters. Key Concepts Vacuoles often represent much of the volume of a plant cell. As components of the endomembrane system, vacuoles are derived from the endoplasmic reticulum and/or Golgi complex. Depending on their function and contents, plant vacuoles fall into two categories: lytic vacuoles (LVs) or protein storage vacuoles (PSVs). LVs, whose contents are acidic and dominated by degradative enzymes, primarily serve a lysosomal function. Protein storage vacuoles (PSVs), whose contents are less acidic and dominated by storage proteins, primarily serve a depot function. Bounded by membranes rich in water channels (aquaporins) that enable rapid osmotic equilibration between the vacuole lumen and cytosol, vacuoles are crucial for establishing and maintaining cell turgor and for ensuring adequate hydration of the cytosol. Plant vacuoles are vital for the temporary storage of both organic and inorganic nutrients and for maintaining their levels within the ranges compatible with metabolism in the cytosol and other intracellular organelles. The plant vacuolar membrane (tonoplast) is unusual in containing two distinct categories of proton pumps – V‐type H + ‐ATPases (V‐ATPases) and vacuolar H + ‐pyrophosphatases (V‐PPases) – that are capable of contributing to vacuolar acidification and to the establishment of the transmembrane H + ‐electrochemical gradient (proton motive force, PMF) required for secondary active solute transport into and out of the vacuole. As the sole enzyme in plant cells capable of catalysing the direct hydrolysis of cytosolic inorganic pyrophosphate (PPi) to inorganic phosphate (Pi), the hydrolytic activity of the V‐PPase is critical if cytosolic biosynthetic reactions that generate PPi are to be sustained. Vacuoles enable plant cells to accumulate both endogenous and exogenous toxins, for instance secondary metabolites and heavy metals, to levels that would be lethal if the same substances were to accumulate to similar levels in the cytosol or other intracellular compartments. Multidrug and toxin efflux (MATE) transporters and ATP‐binding cassette (ABC) transporters mediate the vacuolar uptake of many secondary metabolites and xenobiotics.

show abstract

Membrane‐Bound Pyrophosphatases

Kellosalo

Goldman

2015

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

Membrane‐bound pyrophosphatases (M‐PPases) are homodimeric enzymes that couple the vectorial transport of protons and/or sodium ions to pyrophosphate (PP i ) hydrolysis or synthesis. They are found in prokaryotes, plants, and protists and are thus present in all three domains of life. M‐PPases have an important role in conferring tolerance against abiotic stress conditions and are also vital for plant maturation. Like many proteins that catalyze the formation or cleavage of phosphoanhydride bonds (e.g., P‐ and F‐type ATPases, soluble PPases), M‐PPases require magnesium for activity, both because they bind 2–3 free Mg 2+ ions and because the catalytically relevant substrate at physiological pH and Mg ion concentration is Mg 2 PP i . Besides this alkaline earth metal, M‐PPases also bind alkali metals: Na + ‐pumping M‐PPases bind and transport Na + and certain M‐PPases bind and are activated by K + . In this article, we give a concise summary of the current structural and functional understanding of M‐PPases, with an emphasis on describing the role of the metal ions in the enzymatic function of these proteins.

show abstract

Keep an Eye on PPi: The Vacuolar-Type H+-Pyrophosphatase Regulates Postgerminative Development inArabidopsis

Cited by 147 publications

References 63 publications

The Phosphate Fast-Responsive Genes PECP1 and PPsPase1 Affect Phosphocholine and Phosphoethanolamine Content

The Phosphate Fast-Responsive Genes PECP1 and PPsPase1 Affect Phosphocholine and Phosphoethanolamine Content

Plant Vacuoles

Membrane‐Bound Pyrophosphatases

Contact Info

Product

Resources

About